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REVIEW article

Front. Allergy, 08 July 2021
Sec. Allergens
Volume 2 - 2021 | https://doi.org/10.3389/falgy.2021.676903

Seafood Allergy in Asia: Geographical Specificity and Beyond

  • 1Department of Paediatrics, Faculty of Medicine, The Chinese University of Hong Kong, Hong Kong, China
  • 2Hong Kong Hub of Paediatric Excellence, The Chinese University of Hong Kong, Hong Kong, China

Asian countries have unique ways of food processing and dietary habits that may explain the observed differences in the prevalence, natural history, epidemiology and sensitization pattern of food allergic diseases when compared to western countries. Per capita consumption of seafood, including fish and shellfish, is well above the global average for many Asian countries because of their coastal geographical location and rich seafood supply. The wide availability and high abundance of seafood in Asian countries have shaped a diverse way of processing and eating this major food group. Such unique features have significant impact on the sensitization profile and allergenicity of Asians to fish and shellfish. For example, fish and shellfish are eaten raw in some countries that may promote sensitization to heat-labile allergens not otherwise seen in other regions. Fermented fish sauce is commonly used as a condiment in some countries which may promote fish sensitization. Shrimp head and shrimp roe are regarded as delicacies in some countries, but their allergen profiles are yet to be characterized. Freshwater fish and shellfish are a common food source in many Asian countries but the allergenicity of many such species remains unknown. In this review, we discuss factors that may contribute to differences in molecular profile and sensitization pattern for fish and shellfish that are observed in Asian populations and revisit the current status of seafood allergy in this part of the world. Acknowledging the similarities and differences of seafood allergy patterns between Asian and western populations can help us refine a better strategy for diagnosing and managing seafood allergy.

Introduction

Food allergy is a common allergic disease that affects up to 10% of the population, and its prevalence has been increasing over the past decades (1, 2). While the “big eight” food groups account for 90% of reported allergic reactions (3), the most common triggers of food allergic reactions in a particular geographical location are largely influenced by the feeding pattern, dietary habit and food availability (4). Per capita consumption of seafood, including fish and shellfish, is much higher in Asia when compared to the global average. Asian countries consumed two-thirds of global seafood production (5). In light of this, it is not surprising that seafood allergy is of high importance in Asia where its prevalence was up to 7.7% in some countries (6). Furthermore, Asian countries have distinct ways of seafood processing and dietary habits, which may account for substantial differences observed in the natural history and sensitization profile of seafood allergic subjects when compared to western countries. For example, fish is introduced early into the infants' diet that parallels the younger age at onset of fish allergy in Asian children (7). Seafood is often consumed raw in Asian cuisines, and this eating practice can promote sensitization to heat-sensitive seafood allergens which is not reported in western countries. Besides, Asians consume some seafood species that are not being consumed in other parts of the world. With the advancement of molecular allergology, we are now able to examine allergen components in depth. Emerging studies have reported the occurrence of monosensitization to particular seafood species in this region. In this review, we discuss seafood allergy from the Asian perspective. Acknowledging important differences between East and West and unique features of seafood allergy in Asia would provide important insight on the clinical management of seafood allergy.

Prevalence and Natural History of Seafood Allergy in Asia

Prevalence of Shellfish Allergy in Asian Countries

Shellfish is one of the most common food allergen sources in Asia (Table 1), and the leading cause of food allergy in Taiwan (18, 19), Thailand (20), Singapore (21), Vietnam (9, 12) and Hong Kong (22). In a survey in which IgE sensitization and skin prick tests were used to determine food allergy prevalence, shrimp was found to be the most commonly sensitized food allergen source in Hong Kong, China and India (8). Up to 13.1 and 10.3% of the Chinese and Indian populations had shrimp-specific IgE (sIgE) that exceeded 0.70 kUA/L, while over 2% of the Hong Kong population was positive to shrimp by skin prick test. On the other hand, shellfish allergy is less common in East Asia where shellfish only accounted for 3.4% of all reported food allergy cases in Japan (23) and 0.87% of parent-reported shellfish allergy in South Korea (13). The prevalence of shellfish allergy was affected by environmental exposures, dietary habits and cross-sensitization with other arthropods such as dust mite or cockroaches (24, 25).

TABLE 1
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Table 1. Population-based survey on the prevalence of seafood allergy in Asian countries over the past 10 years.

Prevalence of Fish Allergy in Asian Countries

Fish allergy is less common in Asia than shellfish allergy, but its prevalence is still considerably high (Table 1). Fish allergy affected 1.55–1.60% of Vietnamese, which was second to shellfish as the most common type of food allergen source (9, 12). The prevalence of self-reported fish allergy was 2.29% in Philippines where fish is part of the weaning diet and fish sauce widely used as a condiment (26). In contrary, parent-reported fish allergy affected <1.5% of other Asian populations (11, 13, 22, 26). The rates of IgE sensitization to fish were even lower, when none of the 10,681 subjects in China was positive for fish-specific IgE and only 1.2% of subjects in Hong Kong were sensitized to fish (27). Nevertheless, this study only selected cod as the benchmark for sIgE, when this fish species is not popular in many Asia populations. Thus, results from this study probably underestimated the prevalence of fish allergy in Asia.

Natural History of Shellfish Allergy in Asia

Seafood allergy is generally believed to be persistent throughout life despite limited published evidence on its natural history (28). Shellfish allergy had late onset at a median age of 25 years old in Canadians (29), whereas shellfish allergy started much earlier in the Asian population. While shellfish allergy affected 0.1% of children aged 0–5 years in the United states (30), IgE sensitization to shellfish was as high as 10.6% among Singaporean children younger than 3 years of age (31). It was noteworthy that shellfish was the most frequent cause of food allergy in several studies that involved school-age or pre-school Asian children (9, 12, 1822), which was probably attributed to the early introduction of shellfish in the Asian diet. Another possible reason is that exposure to other arthropods like dust mite or cockroach in tropical or subtropical areas of Asia may increase the shellfish allergy through cross-reactive allergens. Shellfish allergy also tends to persist longer as shellfish was reported to be the leading cause of food-induced anaphylaxis in older children and adults in Singapore (32), Hong Kong (33) and Thailand (34). Nevertheless, a Thai study found that 46% of shrimp-allergic patients were able to tolerate shrimp 10 years later, suggesting that some individuals could outgrow shrimp allergy (35). In addition, Ayuso et al. reported greater epitope recognition for shrimp in children than adults, supporting that shrimp sensitization could decrease with age (36). It remains unclear at this stage whether this is a general observation or is limited to some populations.

Natural History of Fish Allergy in Asia

Similar to shellfish allergy, it is generally believed that fish allergy persists throughout life although the relevant evidence is limited. One study suggested that 65.5% of fish-sensitized infants maintained their sensitization at school age (37). Another study reported that the prevalence of fish allergy was slightly higher in American adults (0.9%) than children (0.6%) (38). The same study also found that nearly 40% of adults having fish allergy started to suffer from this allergy in adulthood. Similar findings were reported in Philippines (26). Alternatively, a small study reported that sIgE levels and skin prick test positivity of fish-allergic patients diminished over a 9-year period, and some subjects were able to tolerate fish with lower allergenicity such as tuna and swordfish (39). Longitudinal studies are required to elucidate the natural history of fish allergy. It is also noteworthy that allergenicity of different fish species could vary significantly, and it is important to distinguish between fish-allergic patients with partial tolerance and true resolution of their fish allergy.

Shellfish and Fish Allergen Sources and Allergens

Molecular Characteristics of Shellfish Allergens

The filamentous muscle protein tropomyosin was first identified as a shrimp allergen in 1993 (40), which was subsequently reported to be a pan-allergen among invertebrates including crustaceans, arachnids, insects and mollusks (41). Tropomyosin is a heat-stable allergen that can withstand high temperature, food processing methods including ultrasound and gamma irradiation, and gastric digestion (42). Arginine kinase was identified as another pan-allergen but, in contrast to tropomyosin, this heat-labile protein exhibited reduced IgE reactivity upon thermal and pH treatment (43). Myosin light chain, sarcoplasmic calcium-binding protein, troponin C, triosephosphate isomerase, and fatty acid-binding protein are other shellfish allergens being registered in the WHO/IUIS allergen database, although their physiochemical properties remain largely unknown (44, 45). Paramyosin was identified as an allergen in mollusk that have limited cross-reactivity with allergens in crustaceans (46).

Molecular Characteristics of Fish Allergens

The calcium-binding muscle protein parvalbumin was first identified as the major fish allergen more than 50 years ago (47). It is highly conserved across all bony fishes (48). Similar to tropomyosin, parvalbumin was resistant to thermal treatment and enzymic hydrolysis (47). Despite high homology across fish species, parvalbumin had different allergenicity in different fish species (48), and the allergenicity of individual fish species was also dependent on the quantity of parvalbumin present in the muscle (49). Collagen was identified as the second heat-stable fish allergen from muscle and skin of fishes (50, 51), but its allergenicity and characteristics were only studied in a small number of fish species. Two heat-labile muscle enzymes of fish, aldolase and enolase, were recently identified as allergens but their clinical relevance remained unclear (52). Tropomyosin was also registered as a fish allergen in the WHO/IUIS database, although its allergenicity has only been demonstrated in one fish species, the Mozambique tilapia. Apart from muscle proteins, fish roe was also reported to cause allergic reactions due to the presence of yolk protein vitellogenin (53).

Major Shrimp Allergens in the Asian Population

Seawater shrimps such as Penaeus monodon and Litopenaeus vannamei are the most widely distributed and marketed shrimps in the world, and their respective allergen profiles have been well-characterized (Table 2). Freshwater shrimps are also popularly consumed in Asia, including the giant freshwater prawn Macrobrachium rosenbergii in Thailand and Taiwan and the freshwater Siberian prawn Exopalaemon modestus in China, Korea and Taiwan. Tropomyosin was identified as the major shrimp allergen, and tropomyosins of freshwater and seawater shrimps shared over 95% sequence homology (54, 55). Arginine kinase and glyceraldehyde 3-phosphate dehydrogenase (GAPDH), on the other hand, were identified as major shrimp allergens in M. rosenbergii, with arginine kinase being cross-reactive with Gryllus bimaculatus (field cricket) (56, 57). Interestingly, the oxygen-transport protein hemocyanin was found to be a species-specific allergen in M. rosenbergii. Hemocyanins of tiger shrimp and mud crab was unable to inhibit IgE binding to M. rosenbergii hemocyanin (58), while a Thai study reported isolated sensitivity to M. rosenbergii based on results of oral food challenges (59).

TABLE 2
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Table 2. Summary of shellfish and fish allergens.

Major Crab Allergens in the Asian Population

Crab is another popular crustacean food item worldwide. In China, crab was the most common culprit for severe adverse food reactions caused by shellfish (8). Crab was also the most common food allergen source among Taiwanese schoolchildren while 16.2% of Singaporean adults had crab allergy (60). The more commonly consumed crabs in western countries include blue crab (Callinectes sapidus), snow crab (Chionoecetes opilio), Dungeness crab (Cancer magister), edible crab (Cancer pagurus) and king crab (Paralithodes camtschaticus) (21, 61), while Chinese mitten crab (Eriocheir sinensis), mud crabs (Scylla paramamosain, Scylla serreta, and Scylla tranquebarica), red crab (Charybdis feriatus) and blue crab (Portunus pelagicus) were more popularly consumed in Asia. The IgE-binding proteins of these latter crab species have been extensively studied (6266). Unlike shrimps, both tropomyosin and arginine kinase are major allergens in crab (Table 2). Arginine kinase is a 41 kDa phosphagen kinase that plays an important role in cellular energy metabolism in invertebrates. Apart from these two major allergens, sarcoplasmic calcium-binding protein, triosephosphate isomerase, pyruvate kinase 2, myosin light chain I and filamin C were minor crab allergens (56, 67, 68). Jasim et al. (69) identified three common crab allergens including tropomyosin, arginine kinase and actin as well as a novel allergen hemocyanin from S. transquebarica that is commonly consumed in Malaysia.

Major Mollusk Allergens in the Asian Population

Besides crustaceans such as shrimp and crab, mollusks are popular food item in Asian countries. There is a common belief that mollusks offer health-promoting effects because of their rich vital nutrients and active secondary metabolites (70). Cross-reactivity between crustaceans and mollusks were well-recognized (42). Despite this, Suzuki et al. (46) identified a 100 kDa myofibrillar protein paramyosin in the disc abalone Haliotis discus as a novel allergen. This protein reacted with 16 of the 18 Japanese sera from allergic subjects being studied. They also reported IgE reactivity against paramyosins from turban shell, mussel, scallop, squid and octopus, which was subsequently found in the Asian rapa whelk Rapana venosa (71). Interestingly, paramyosin is a heat-labile protein so the clinical relevance of paramyosin would be limited to some Asian populations such as Japanese and Koreans where mollusks and abalone are served as sashimi.

Major Echinoderm Allergens in Asian Population

Although phylogenetically distinct from crustaceans, mollusks and fin fish, echinoderms including starfish, sea cucumbers and sea urchins are also popular seafood delicacies in China, Japan and Korea. For instance, Japanese consume eggs of starfish and sea urchin roe called “uni.” Worldwide consumption of sea urchin has been increasing, and several case reports of anaphylaxis to sea urchin roe or upon stinging by starfish were published (72, 73). A 118-kDa protein in sea urchin roe was presented as a potential allergen by immunoblotting, which was identified as major yolk protein by MALDI-TOF mass spectrometry (74).

Insect Consumption and Cross-Reactivity With Shrimp

Insects have become a unique diet in China under the cultural influence of traditional Chinese food and medicine. The consumption of oil-fried, water-boiled or ground silkworm pupa is common in China whereas silkworms have been used as therapeutics in traditional medicine and also commonly consumed after boiling with soybean sauce in Korea. Although insects are not widely consumed in western countries at present, edible insects have gained attention as a novel and sustainable food for protein sources worldwide due to the worry about food scarcity.

However, there is increasing recognition about allergy to insects. From 1980 to 2007, 61 (17%) of 358 reported cases of anaphylaxis were triggered by insects including silkworm pupas, cicada pupas, grasshoppers, locusts and hawkmoth (75). Over 1,000 patients experienced anaphylactic reactions following consumption of silkworm pupa annually in China, and foreign tourists also experienced anaphylactic shock after eating silkworm (76). Considering tropomyosin as a pan-allergen in invertebrates including crustaceans, mollusks, dust mites and cockroaches, shrimp-allergic patients are at risk of insect allergy due to cross-reactivity between allergens. As early as 1996, Leung et al. reported co-sensitization among insects, cockroach, fruit fly and shrimp (77). More recently, Jeong et al. (78) reported among 15 patients diagnosed with silkworm pupa allergy that 11 (73.3%) exhibited sIgE reactivity to shrimp and crab by ImmunoCAP (≥0.35 kUA/L) and 53.3% of patients' sera reacted to silkworm pupa tropomyosin. Kamemura et al. (79) also demonstrated strong positive correlation between shrimp- and cricket-specific IgE responses by the IgE crosslinking-induced luciferase expression (EXiLE) assay. Similarly, Broekman et al. (80) showed that all 15 shrimp-allergic patients were also sensitized to mealworm. There was similar basophil reactivity of these shrimp-allergic patients to all tested insect species including mealworm, cricket, grasshopper and moth. By means of immunoblot and nano LC-MS/MS analyses, insect extracts were found to contain a considerable number of arthropod allergens including tropomyosin, arginine kinase, myosin light chain and triosephosphate isomerase. These allergens probably accounted for cross-reactivity between shrimp and insects. Therefore, some shrimp-allergic subjects may also be allergic to insects.

Major Fish Allergens in Asian Population

Unlike shrimp and crab where regional availability largely governs the species consumed, many fish species such as cod, salmon and tuna were distributed and consumed worldwide. In addition to these imported species, many inland Asian countries rely on freshwater aquaculture. Freshwater fishes such as carp, tilapia and catfish are stable food sources in many Asian populations. Freshwater fishes usually have a muddy taste and contain bacteria and parasites that impose food safety concern when they are eaten raw. Heat-labile fish allergens such as enolase and aldolase may thus be less relevant in allergy to freshwater fishes (Table 2). Our team has recently identified parvalbumin as the major allergen Cten i 1 in grass carp (Ctenopharyngodon idella) using sera from 69 subjects with IgE-mediated fish allergy (81). Ctenopharyngodon idella is the most commonly consumed freshwater fish species in Hong Kong, which is phylogenetically close to the common carp (Cyprinus carpio). By inhibition ELISA, we neatly illustrated stronger IgE inhibitory effect against Cten i 1 by Cyp c 1 (parvalbumin from common carp, ~80% inhibition) when compared to Gad m 1 (parvalbumin of codfish) and Sal s 1 (parvalbumin of salmon). These findings could be explained by stronger allergenicity for parvalbumin of freshwater fishes than seawater fishes and/or stronger avidity of IgE to freshwater fish parvalbumin. On the other hand, Reuthers et al. (82) analyzed the IgE reactivity of 16 freshwater fishes available in Vietnam with sera from 18 Australian and three European patients with history of fish allergy. Concordantly, parvalbumin was found to be the major allergen in all freshwater fishes. Several isoforms of parvalbumin were detected in most fish species.

Apart from parvalbumin, Liu et al. (83) detected IgE binding in 10 proteins sized from 17 to 114 kDa from tilapia (Oreochromis mossambicus). The sensitization rate of subjects to these proteins ranged from 20 to 80%. All patients reacted a 32 kDa-protein which was identified as tropomyosin (Ore m 4) by LC-ES-MS/MS. Ore m 4 shared 58.8% sequence similarity as tropomyosin from northern shrimp, but 87.7% homology with human tropomyosin isoform 5. It should be noted that any protein resembling human proteins appear to have limited allergenic potential. In this patient group, 6 of 10 subjects suffered from inflammatory bowel disease (IBD). It is possible that anti-tropomyosin IgE antibody cross-reacted with gut proteins to result in IBD. It also raised a query if tropomyosin is a clinically relevant allergen in fish allergy.

Effect of Unique Dietary Habits in Asian Population to Allergen Sensitization Profile

Raw Fish Consumption and Collagen Sensitization

Collagen was first identified as a fish allergen in a Japanese study (50), and subsequently regarded as a pan-allergen in this population. Half of 36 fish-allergic Japanese patients reacted to collagen extracted from Pacific mackerel, in comparison to only 16 (44%) patients who were positive to parvalbumin (84). In addition, 13 (36%) subjects were mono-sensitized to collagen. Collagen from Pacific mackerel also significantly inhibited IgE binding to heated crude extract of 22 fish species by 87–93%. In contrast, the sensitization rate to collagen was low in European and Australian populations (52, 85). This much higher rate of collagen sensitization together with strong IgE inhibition in Japanese might be explained by their traditional dietary practice of eating raw fish sashimi or sushi. The risk of collagen sensitization was low in cooked fish, while the insoluble intact collagen found in raw fish might be a potent sensitizing allergen due to its resistance to gastric acid digestion (84).

Fish Roe Consumption and Vitellogenin Sensitization

Fish roes are nutritious food commonly consumed in Japan. Salmon roe, also known as salmon caviar, red caviar, rainbow trout roe and ikra, is a common Japanese cuisine. Fish roe is the fifth most common food allergen source in Japan, and it is mandatory in the Japanese food sanitation law to label fish roe as a possible food allergen. In a retrospective study, half of 68 Japanese subjects reacted to salmon roe on oral food challenge (86). Analysis of sera collected from 20 patients with salmon roe allergy found that β'-component (β'-c) was the major allergen (53). Nine (45%) of 21 sera reacted to lipovitellin. Both lipovitellin and β'-c are degradation fragments of vitellogenin which issynthesized in fish liver and carried to oocytes through bloodstream. β'-c was also characterized as a major fish roe allergen in teleostean such as large yellow croaker (Pseudosciaena crocea) that is widely consumed in China (87). In the contrary, fish roe allergy is rare in western countries. When there is popular consumption of fish roes from sturgeon, paddlefish, cod, lumpfish, capelin, herring and salmon worldwide, there were increasing number of cases with fish roe allergy in USA, Portugal, Spain and Finland (8891).

Crustacean Body Parts Consumption Leading to Diversified Allergen Sensitization

Over the past decades, we found more reports on the profiling and characterization of allergens from shrimp as a prototype for shellfish. Tropomyosin has long been regarded as a major crustacean allergen. Over 80% of European shellfish-allergic subjects were sensitized to tropomyosin (92, 93). However, our recent study suggested that only slightly over half of subjects with challenge-proven shrimp allergy were sensitized to tropomyosin (94). Such low sensitization rate to tropomyosin was also reported in Thai (34.2%) and Japanese (37%) (95, 96), supporting that tropomyosin might not be the major allergen in Asians. We further demonstrated that Chinese patients were sensitized to multiple shrimp allergens, with troponin C and fatty acid-binding protein being the major allergens (97, 98).

One possible reason for such diversified sensitization profiles in different Asian populations might be due to the consumption practice for non-muscle body parts of shrimp and crab. While western populations mainly consume muscle of shelled shrimps, shrimp is always served head-on and shell-on in East and Southeast Asia when the shell, cephalothorax (containing brain, heart, stomach and bladder), ovaries and hepatopancreas are consumed together with shrimp muscle. The best example is hemocyanin that is found mainly in shrimp cephalothorax but not muscle. In addition, Khanaruksombat et al. (99) reported novel allergens from muscle, shell, hepatopancreas and ovaries of banana shrimp, Fenneropenaeus merguiensis, that is commonly consumed in Thailand. They detected four immunoreactive bands from shell extract and six immunoreactive bands from ovarian extracts at different vitellogenic stages. On top of arginine kinase and sarcoplasmic calcium-binding protein, these investigators identified a novel allergen called glyceraldehyde-3-phosphate dehydrogenase from the shell. Interestingly, different allergens including vitellogenin, ovarian peritrophin 1 precursor, β-actin and 14-3-3 protein were detected at different stages of ovarian development. It is noteworthy that vitellogenin is a female specific protein also found in the hemolymph of most crustacean species, and its degradation fragments lipovitellin and β'-c were defined as major fish roe allergens. This study highlighted the presence of IgE-binding proteins in both shrimp muscle and organs.

Fermented Shrimp Processing and Its Effect on Shrimp Allergenicity

Fermented foods such as kimchi and saeujeot, a salted and fermented shrimp product, are popular food items in Korea and some other Asian countries. Saeujeot is ripened primarily by proteolytic enzymes present in shrimp, and this process confers characteristic flavor and aroma in this food item. Although being heat stable, the allergenicity of tropomyosin decreased during fermentation of shrimps. Park et al. (100) demonstrated that tropomyosin could not be detected after 6 days of fermentation at 25°C, 10 days at 15°C and 30 days at 5°C. More importantly, the binding ability of tropomyosin in saeujeot to patient sera decreased gradually during fermentation process. This binding ability decreased further and faster at higher fermentation temperature, which might be caused by the activity of a trypsin-like enzyme that decomposes tropomyosin. Kim et al. (101) further investigated the allergenicity of saeujeot at various temperatures (25, 15, and 5°C) and salt concentrations (25, 15, and 10%). They showed that the binding ability of tropomyosin decreased faster at higher temperature and lower salt concentration. During fermentation, the allergenicity of saeujeot increased initially as tropomyosin dissolves in salt, while it is subsequently decomposed by enzymes.

Future Perspectives

The clinical features of seafood allergy in Asia are distinct from the rest of the world. It is important to acknowledge such differences and to adapt our management strategies accordingly. As illustrated in peanut allergy, the key allergenic components were different in populations with high and low prevalences of peanut allergy (102). In shellfish, tropomyosin might be the key allergen in western cohorts while it is important to include other allergens such as troponin C and fatty acid-binding protein in Asians (62, 63). Fish collagen or other heat-labile proteins such as enolase and aldolase would be useful in fish allergy diagnosis in regions where raw fish consumption is common. We have also learnt that shrimp cephalothorax and fish roe can be important allergen sources, and these extracts should be standardized and made available for the clinical diagnosis of seafood allergy. In this review, we illustrated how the diagnosis of seafood allergy can be improved by studying clinically relevant or diet-related species in patients with mono-sensitization to specific seafood species. The advancement of molecular allergology prompted the identification of novel or species-specific allergens that allows us to derive more comprehensive panels for component-resolved diagnosis. Novel diagnostic platforms such as basophil activation test or EXiLE assays can also be adopted to test in-house allergen extracts in a standardized manner (94). Nonetheless, there are knowledge gaps over the prevalence and natural history of seafood allergy in Asian adults as well as the roles that dust mites and other environmental factors play in primary allergen sensitization. More challenge-based studies are also needed to identify novel seafood allergens in this region. These new scientific evidences will ultimately improve our clinical management strategies for seafood allergy.

Author Contributions

CW and NL prepared the manuscript. AL, GW, and TL critically revised the manuscript. All authors contributed to manuscript revision, read, and approved the submitted version.

Funding

This manuscript was funded by Research Impact Fund (reference no. R4035-19) of Research Grants Council, Hong Kong. The funder did not participate in the data collection, manuscript drafting and decision for its submission. The open access publication fee of this manuscript was supported by private fund of the corresponding author at the Chinese University of Hong Kong.

Conflict of Interest

The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest.

References

1. Sicherer SH, Sampson HA. Food allergy: a review and update on epidemiology, pathogenesis, diagnosis, prevention, and management. J Allergy Clin Immunol. (2018) 141:41–58. doi: 10.1016/j.jaci.2017.11.003

PubMed Abstract | CrossRef Full Text | Google Scholar

2. Gupta RS, Warren CM, Smith BM, Jiang J, Blumenstock JA, Davis MM, et al. Prevalence and severity of food allergies among US adults. JAMA Netw Open. (2019) 2:e185630. doi: 10.1001/jamanetworkopen.2018.5630

PubMed Abstract | CrossRef Full Text | Google Scholar

3. Boye JI. Food allergies in developing and emerging economies: need for comprehensive data on prevalence rates. Clin Transl Allergy. (2012) 2:25. doi: 10.1186/2045-7022-2-25

PubMed Abstract | CrossRef Full Text | Google Scholar

4. Loh W, Tang MLK. The epidemiology of food allergy in the global context. Int J Environ Res Public Health. (2018) 15:2043. doi: 10.3390/ijerph15092043

PubMed Abstract | CrossRef Full Text | Google Scholar

5. Hosomi R, Yoshida M, Fukunaga K. Seafood consumption and components for health. Glob J Health Sci. (2012) 4:72–86. doi: 10.5539/gjhs.v4n3p72

CrossRef Full Text | Google Scholar

6. Davis CM, Gupta RS, Aktas ON, Diaz V, Kamath SD, Lopata AL. Clinical management of seafood allergy. J Allergy Clin Immunol Pract. (2020) 8:37–44. doi: 10.1016/j.jaip.2019.10.019

CrossRef Full Text | Google Scholar

7. Lee AJ, Thalayasingam M, Lee BW. Food allergy in Asia: how does it compare? Asia Pac Allergy. (2013) 3:3–14. doi: 10.5415/apallergy.2013.3.1.3

CrossRef Full Text | Google Scholar

8. Li J, Ogorodova LM, Mahesh PA, Wang MH, Fedorova OS, Leung TF, et al. Comparative study of food allergies in children from China, India, and Russia: the EuroPrevall-INCO surveys. J Allergy Clin Immunol Pract. (2020) 8:1349–58. doi: 10.1016/j.jaip.2019.11.042

PubMed Abstract | CrossRef Full Text | Google Scholar

9. Le TTK, Tran TTB, Ho HTM, Vu ATL, McBryde E, Lopata AL. The predominance of seafood allergy in Vietnamese adults: results from the first population-based questionnaire survey. World Allergy Organ J. (2020) 13:100102. doi: 10.1016/j.waojou.2020.100102

PubMed Abstract | CrossRef Full Text | Google Scholar

10. Dai H, Wang F, Wang L, Wan J, Xiang Q, Zhang H, et al. An epidemiological investigation of food allergy among children aged 3 to 6 in an urban area of Wenzhou, China. BMC Pediatr. (2020) 20:220. doi: 10.1186/s12887-020-02115-8

PubMed Abstract | CrossRef Full Text | Google Scholar

11. Ziyab AH. Prevalence of food allergy among schoolchildren in Kuwait and its association with the coexistence and severity of asthma, rhinitis, and eczema: a cross-sectional study. World Allergy Organ J. (2019) 12:100024. doi: 10.1016/j.waojou.2019.100024

PubMed Abstract | CrossRef Full Text | Google Scholar

12. Le TTK, Tran TTB, Ho HTM, Vu ATL, Lopata AL. Prevalence of food allergy in Vietnam: comparison of web-based with traditional paper-based survey. World Allergy Organ J. (2018) 11:16. doi: 10.1186/s40413-018-0195-2

PubMed Abstract | CrossRef Full Text | Google Scholar

13. Kim M, Lee JY, Jeon HY, Yang HK, Lee KJ, Han Y, et al. Prevalence of immediate-type food allergy in Korean schoolchildren in 2015: a nationwide, population-based study. Allergy Asthma Immunol Res. (2017) 9:410–6. doi: 10.4168/aair.2017.9.5.410

PubMed Abstract | CrossRef Full Text | Google Scholar

14. Park M, Kim D, Ahn K, Kim J, Han Y. Prevalence of immediate-type food allergy in early childhood in Seoul. Allergy Asthma Immunol Res. (2014) 6:131–6. doi: 10.4168/aair.2014.6.2.131

PubMed Abstract | CrossRef Full Text | Google Scholar

15. Dey D, Ghosh N, Pandey N, Bhattacharya SG. A hospital-based survey on food allergy in the population of Kolkata, India. Int Arch Allergy Immunol. (2014) 164:218–21. doi: 10.1159/000365629

PubMed Abstract | CrossRef Full Text | Google Scholar

16. Lao-araya M, Trakultivakorn M. Prevalence of food allergy among preschool children in northern Thailand. Pediatr Int. (2012) 54:238–43. doi: 10.1111/j.1442-200X.2011.03544.x

PubMed Abstract | CrossRef Full Text | Google Scholar

17. Ho MH, Lee SL, Wong WH, Ip P, Lau YL. Prevalence of self-reported food allergy in Hong Kong children and teens - a population survey. Asian Pac J Allergy Immunol. (2012) 30:275–84.

PubMed Abstract | Google Scholar

18. Wu TC, Tsai TC, Huang CF, Chang FY, Lin CC, Huang IF, et al. Prevalence of food allergy in Taiwan: a questionnaire-based survey. Intern Med J. (2012) 42:1310–5. doi: 10.1111/j.1445-5994.2012.02820.x

PubMed Abstract | CrossRef Full Text | Google Scholar

19. Hsin YC, Hsin YC, Huang JL, Yeh KW. Clinical features of adult and pediatric anaphylaxis in Taiwan. Asian Pac J Allergy Immunol. (2011) 29:307–12.

PubMed Abstract | Google Scholar

20. Lertnawapan R, Maek-a-nantawat W. Anaphylaxis and biphasic phase in Thailand: 4-year observation. Allergol Int. (2011) 60:283–9. doi: 10.2332/allergolint.10-OA-0256

PubMed Abstract | CrossRef Full Text | Google Scholar

21. Thong BY, Cheng YK, Leong KP, Tang CY, Chng HH. Immediate food hypersensitivity among adults attending a clinical immunology/allergy centre in Singapore. Singapore Med J. (2007) 48:236–40.

PubMed Abstract | Google Scholar

22. Leung TF, Yung E, Wong YS, Lam CW, Wong GW. Parent-reported adverse food reactions in Hong Kong Chinese pre-schoolers: epidemiology, clinical spectrum and risk factors. Pediatr Allergy Immunol. (2009) 20:339–46. doi: 10.1111/j.1399-3038.2008.00801.x

PubMed Abstract | CrossRef Full Text | Google Scholar

23. Ebisawa M, Ito K, Fujisawa T. Committee for Japanese Pediatric Guideline for Food Allergy, The Japanese Society of Pediatric Allergy and Clinical Immunology. Japanese guidelines for food allergy 2020. Allergol Int. (2020) 69:370–86. doi: 10.1016/j.alit.2020.03.004

PubMed Abstract | CrossRef Full Text | Google Scholar

24. Tham EH, Leung DYM. How different parts of the world provide new insights into food allergy. Allergy Asthma Immunol Res. (2018) 10:290–9. doi: 10.4168/aair.2018.10.4.290

PubMed Abstract | CrossRef Full Text | Google Scholar

25. Wai CYY, Leung NYH, Chu KH, Leung PSC, Leung ASY, Wong GWK, et al. Overcoming shellfish allergy: how far have we come? Int J Mol Sci. (2020) 21:2234. doi: 10.3390/ijms21062234

PubMed Abstract | CrossRef Full Text | Google Scholar

26. Connett GJ, Gerez I, Cabrera-Morales EA, Yuenyongviwat A, Ngamphaiboon J, Chatchatee P, et al. A population-based study of fish allergy in the Philippines, Singapore and Thailand. Int Arch Allergy Immunol. (2012) 159:384–90. doi: 10.1159/000338940

PubMed Abstract | CrossRef Full Text | Google Scholar

27. Lv Z, Wang J, Chen Z, Chen X, Zhang L, Li C, et al. Temperature regulations impose positive influence on the biomethane potential versus digesting modes treating agricultural residues. Bioresour Technol. (2020) 301:122747. doi: 10.1016/j.biortech.2020.122747

PubMed Abstract | CrossRef Full Text | Google Scholar

28. Sicherer SH, Sampson HA. Food allergy: epidemiology, pathogenesis, diagnosis, and treatment. J Allergy Clin Immunol. (2014) 133:291–307. doi: 10.1016/j.jaci.2013.11.020

PubMed Abstract | CrossRef Full Text | Google Scholar

29. Ben-Shoshan M, Harrington DW, Soller L, Fragapane J, Joseph L, St Pierre Y, et al. A population-based study on peanut, tree nut, fish, shellfish, and sesame allergy prevalence in Canada. J Allergy Clin Immunol. (2010) 125:1327–35. doi: 10.1016/j.jaci.2010.03.015

PubMed Abstract | CrossRef Full Text | Google Scholar

30. Sicherer SH, Munoz-Furlong A, Sampson HA. Prevalence of seafood allergy in the United States determined by a random telephone survey. J Allergy Clin Immunol. (2004) 114:159–65. doi: 10.1016/j.jaci.2004.04.018

PubMed Abstract | CrossRef Full Text | Google Scholar

31. Khoo J, Shek LP, Khor ES, Wang DY, Lee BW. Pattern of sensitization to common environmental allergens amongst atopic Singapore children in the first 3 years of life. Asian Pac J Allergy Immunol. (2001) 19:225–9.

PubMed Abstract | Google Scholar

32. Thong BY, Cheng YK, Leong KP, Tang CY, Chng HH. Anaphylaxis in adults referred to a clinical immunology/allergy centre in Singapore. Singapore Med J. (2005) 46:529–34.

PubMed Abstract | Google Scholar

33. Smit DV, Cameron PA, Rainer TH. Anaphylaxis presentations to an emergency department in Hong Kong: incidence and predictors of biphasic reactions. J Emerg Med. (2005) 28:381–8. doi: 10.1016/j.jemermed.2004.11.028

PubMed Abstract | CrossRef Full Text | Google Scholar

34. Piromrat K, Chinratanapisit S, Trathong S. Anaphylaxis in an emergency department: a 2-year study in a tertiary-care hospital. Asian Pac J Allergy Immunol. (2008) 26:121–8.

PubMed Abstract | Google Scholar

35. Ittiporn S, Piboonpocanun S, Pacharn P, Visitsunthorn N, Thongngarm T, Jirapongsananuruk O. Natural resolution of non-anaphylactic shrimp allergy in patients diagnosed 10 years earlier by oral food challenge. Asian Pac J Allergy Immunol. (2019). doi: 10.12932/AP-080119-0470. [Epub ahead of print].

PubMed Abstract | CrossRef Full Text | Google Scholar

36. Ayuso R, Sanchez-Garcia S, Lin J, Fu Z, Ibanez MD, Carrillo T, et al. Greater epitope recognition of shrimp allergens by children than by adults suggests that shrimp sensitization decreases with age. J Allergy Clin Immunol. (2010) 125:1286–93. doi: 10.1016/j.jaci.2010.03.010

PubMed Abstract | CrossRef Full Text | Google Scholar

37. Priftis KN, Mermiri D, Papadopoulou A, Papadopoulos M, Fretzayas A, Lagona E. Asthma symptoms and bronchial reactivity in school children sensitized to food allergens in infancy. J Asthma. (2008) 45:590–5. doi: 10.1080/02770900802032941

PubMed Abstract | CrossRef Full Text | Google Scholar

38. Sicherer SH, Warren CM, Dant C, Gupta RS, Nadeau KC. Food allergy from infancy through adulthood. J Allergy Clin Immunol Pract. (2020) 8:1854–64. doi: 10.1016/j.jaip.2020.02.010

CrossRef Full Text | Google Scholar

39. Stavroulakis G, Giavi S, Douladiris N, Manousakis M, Papadopoulos NG. Fish allergy - natural history and crossreactivity between fish species. Clin Transl Allergy. (2011) 1:O26. doi: 10.1186/2045-7022-1-S1-O26

CrossRef Full Text | Google Scholar

40. Shanti KN, Martin BM, Nagpal S, Metcalfe DD, Rao PV. Identification of tropomyosin as the major shrimp allergen and characterization of its IgE-binding epitopes. J Immunol. (1993) 151:5354–63.

PubMed Abstract | Google Scholar

41. Reese G, Ayuso R, Lehrer SB. Tropomyosin: an invertebrate pan-allergen. Int Arch Allergy Immunol. (1999) 119:247–58. doi: 10.1159/000024201

CrossRef Full Text | Google Scholar

42. Leung NY, Wai CY, Shu S, Wang J, Kenny TP, Chu KH, et al. Current immunological and molecular biological perspectives on seafood allergy: a comprehensive review. Clin Rev Allergy Immunol. (2014) 46:180–97. doi: 10.1007/s12016-012-8336-9

PubMed Abstract | CrossRef Full Text | Google Scholar

43. Kamath SD, Rahman AM, Voskamp A, Komoda T, Rolland JM, O'Hehir RE, et al. Effect of heat processing on antibody reactivity to allergen variants and fragments of black tiger prawn: a comprehensive allergenomic approach. Mol Nutr Food Res. (2014) 58:1144–55. doi: 10.1002/mnfr.201300584

PubMed Abstract | CrossRef Full Text | Google Scholar

44. Ruethers T, Taki AC, Johnston EB, Nugraha R, Le TTK, Kalic T, et al. Seafood allergy: a comprehensive review of fish and shellfish allergens. Mol Immunol. (2018) 100:28–57. doi: 10.1016/j.molimm.2018.04.008

PubMed Abstract | CrossRef Full Text | Google Scholar

45. Tong WS, Yuen AW, Wai CY, Leung NY, Chu KH, Leung PS. Diagnosis of fish and shellfish allergies. J Asthma Allergy. (2018) 11:247–60. doi: 10.2147/JAA.S142476

CrossRef Full Text | Google Scholar

46. Suzuki M, Kobayashi Y, Hiraki Y, Nakata H, Shiomi K. Paramyosin of the disc abalone Haliotis discus discus: identification as a new allergen and cross-reactivity with tropomyosin. Food Chemistry. (2011) 124:921–6. doi: 10.1016/j.foodchem.2010.07.020

CrossRef Full Text | Google Scholar

47. Aas K, Elsayed SM. Characterization of a major allergen (Cod) - effect of enzymic hydrolysis on allergenic activity. J Allergy. (1969) 44:333–43. doi: 10.1016/0021-8707(69)90025-2

PubMed Abstract | CrossRef Full Text | Google Scholar

48. Kuehn A, Swoboda I, Arumugam K, Hilger C, Hentges F. Fish allergens at a glance: variable allergenicity of parvalbumins, the major fish allergens. Front Immunol. (2014) 5:179. doi: 10.3389/fimmu.2014.00179

PubMed Abstract | CrossRef Full Text | Google Scholar

49. Kuehn A, Scheuermann T, Hilger C, Hentges F. Important variations in parvalbumin content in common fish species: a factor possibly contributing to variable allergenicity. Int Arch Allergy Immunol. (2010) 153:359–66. doi: 10.1159/000316346

PubMed Abstract | CrossRef Full Text | Google Scholar

50. Hamada Y, Nagashima Y, Shiomi K. Identification of collagen as a new fish allergen. Biosci Biotechnol Biochem. (2001) 65:285–91. doi: 10.1271/bbb.65.285

PubMed Abstract | CrossRef Full Text | Google Scholar

51. Kobayashi Y, Kuriyama T, Nakagawara R, Aihara M, Hamada-Sato N. Allergy to fish collagen: thermostability of collagen and IgE reactivity of patients' sera with extracts of 11 species of bony and cartilaginous fish. Allergol Int. (2016) 65:450–8. doi: 10.1016/j.alit.2016.04.012

PubMed Abstract | CrossRef Full Text | Google Scholar

52. Kuehn A, Hilger C, Lehners-Weber C, Codreanu-Morel F, Morisset M, Metz-Favre C, et al. Identification of enolases and aldolases as important fish allergens in cod, salmon and tuna: component resolved diagnosis using parvalbumin and the new allergens. Clin Exp Allergy. (2013) 43:811–22. doi: 10.1111/cea.12117

PubMed Abstract | CrossRef Full Text | Google Scholar

53. Shimizu Y, Nakamura A, Kishimura H, Hara A, Watanabe K, Saeki H. Major allergen and its IgE cross-reactivity among salmonid fish roe allergy. J Agric Food Chem. (2009) 57:2314–9. doi: 10.1021/jf8031759

PubMed Abstract | CrossRef Full Text | Google Scholar

54. Zhang ZY, Li XM, Xiao H, Nowak-Wegrzyn A, Zhou P. IgE-binding epitope mapping of tropomyosin allergen (Exo m 1) from Exopalaemon modestus, the freshwater Siberian prawn. Food Chem. (2020) 309:125603. doi: 10.1016/j.foodchem.2019.125603

PubMed Abstract | CrossRef Full Text | Google Scholar

55. Kumjim S, Jirapongsananuruk O, Piboonpocanun S. Cloning and characterization of recombinant tropomyosin of giant freshwater shrimp M. rosenbergii to determine major allergens causing allergic reactions among shrimp-allergic children. Asian Pac J Allergy Immunol. (2016) 34:229–35. doi: 10.12932/AP0698

PubMed Abstract | CrossRef Full Text | Google Scholar

56. Wu CC, Lee CH, Tyan YC, Huang ES, Yu WT, Yu HS. Identification of pyruvate kinase 2 as a possible crab allergen and analysis of allergenic proteins in crabs consumed in Taiwan. Food Chem. (2019) 289:413–8. doi: 10.1016/j.foodchem.2019.03.074

PubMed Abstract | CrossRef Full Text | Google Scholar

57. Yadzir ZH, Misnan R, Abdullah N, Bakhtiar F, Arip M, Murad S. Identification of the major allergen of Macrobrachium rosenbergii (giant freshwater prawn). Asian Pac J Trop Biomed. (2012) 2:50–4. doi: 10.1016/S2221-1691(11)60189-5

PubMed Abstract | CrossRef Full Text | Google Scholar

58. Piboonpocanun S, Jirapongsananuruk O, Tipayanon T, Boonchoo S, Goodman RE. Identification of hemocyanin as a novel non-cross-reactive allergen from the giant freshwater shrimp Macrobrachium rosenbergii. Mol Nutr Food Res. (2011) 55:1492–8. doi: 10.1002/mnfr.201000602

PubMed Abstract | CrossRef Full Text | Google Scholar

59. Jirapongsananuruk O, Sripramong C, Pacharn P, Udompunturak S, Chinratanapisit S, Piboonpocanun S, et al. Specific allergy to Penaeus monodon (seawater shrimp) or Macrobrachium rosenbergii (freshwater shrimp) in shrimp-allergic children. Clin Exp Allergy. (2008) 38:1038–47. doi: 10.1111/j.1365-2222.2008.02979.x

PubMed Abstract | CrossRef Full Text | Google Scholar

60. Wan KS, Yang WN, Wu WF. A survey of serum specific-IgE to common allergens in primary school children of Taipei City. Asian Pac J Allergy Immunol. (2010) 28:1–6.

PubMed Abstract | Google Scholar

61. Danquah AO, Boye JI, Simpson BK. Fish and shellfish allergens. In: Joyce I, editor. Allergen Management in the Food Industry. New Jersey, USA: Wiley & Sons (2010). p. 271–87.

Google Scholar

62. Leung PSC, Chen YC, Gershwin ME, Wong SH, Kwan HS, Chu KH. Identification and molecular characterization of Charybdis feriatus tropomyosin, the major crab allergen. J Allergy Clin Immunol. (1998) 102:847–52. doi: 10.1016/S0091-6749(98)70027-2

PubMed Abstract | CrossRef Full Text | Google Scholar

63. Rosmilah M, Shahnaz M, Zailatul HMY, Noormalin A, Normilah I. Identification of tropomyosin and arginine kinase as major allergens of Portunus pelagicus (blue swimming crab). Trop Biomed. (2012) 29:467–78.

PubMed Abstract | Google Scholar

64. Misnan R, Murad S, Yadzir ZHM, Abdullah N. Identification of the major allergens of Charybdis feriatus (red crab) and its cross-reactivity with Portunus pelagicus (blue crab). Asian Pac J Allergy Immunol. (2012) 30:285–93.

PubMed Abstract | Google Scholar

65. Liang YL, Cao MJ, Su WJ, Zhang LJ, Huang YY, Liu GM. Identification and characterisation of the major allergen of Chinese mitten crab (Eriocheir sinensis). Food Chem. (2008) 111:998–1003. doi: 10.1016/j.foodchem.2008.05.023

CrossRef Full Text | Google Scholar

66. Shen YA, Cao MJ, Cai QF, Su WJ, Yu HL, Ruan WW, et al. Purification, cloning, expression and immunological analysis of Scylla serrata arginine kinase, the crab allergen. J Sci Food Agric. (2011) 91:1326–35. doi: 10.1002/jsfa.4322

PubMed Abstract | CrossRef Full Text | Google Scholar

67. Li MS, Xia F, Liu M, He XR, Chen YY, Bai TL, et al. Cloning, expression, and epitope identification of myosin light chain 1: an allergen in mud crab. J Agric Food Chem. (2019) 67:10458–69. doi: 10.1021/acs.jafc.9b04294

PubMed Abstract | CrossRef Full Text | Google Scholar

68. He XR, Cheng YM, Yang Y, Xie JJ, Chu KH, Zhang YX, et al. Cloning, expression and comparison of the properties of Scy p 9, a Scylla paramamosain allergen. Food Funct. (2020) 11:3006–19. doi: 10.1039/D0FO00004C

PubMed Abstract | CrossRef Full Text | Google Scholar

69. Jasim HA, Misnan R, Yadzir ZHM, Abdullah N, Bakhtiar F, Arip M, et al. Identification of common and novel major crab allergens in Scylla tranquebarica and the allergen stability in untreated and vinegar-treated Crab. Iran J Allergy Asthma Immunol. (2021) 20:76–87. doi: 10.18502/ijaai.v20i1.5414

PubMed Abstract | CrossRef Full Text | Google Scholar

70. Khan BM, Liu Y. Marine Mollusks: food with benefits. Compr Rev Food Sci Food Saf. (2019) 18:548–64. doi: 10.1111/1541-4337.12429

CrossRef Full Text | Google Scholar

71. Yu C, Gao X, Lin H, Xu L, Ahmed I, Khan MU, et al. Purification, characterization, and three-dimensional structure prediction of paramyosin, a novel allergen of Rapana venosa. J Agric Food Chem. (2020) 68:14632–42. doi: 10.1021/acs.jafc.0c04418

PubMed Abstract | CrossRef Full Text | Google Scholar

72. Ihama Y, Fukasawa M, Ninomiya K, Kawakami Y, Nagai T, Fuke C, et al. Anaphylactic shock caused by sting of crown-of-thorns starfish (Acanthaster planci). Forensic Sci Int. (2014) 236:E5–E8. doi: 10.1016/j.forsciint.2014.01.001

PubMed Abstract | CrossRef Full Text | Google Scholar

73. Hickey RW. Sea urchin roe (uni) anaphylaxis. Ann Allerg Asthma Im. (2007) 98:493–4. doi: 10.1016/S1081-1206(10)60766-1

PubMed Abstract | CrossRef Full Text | Google Scholar

74. Yamasaki A, Higaki H, Nakashima K, Yamamoto O, Hein KZ, Takahashi H, et al. Identification of a major yolk protein as an allergen in sea urchin roe. Acta Derm Venereol. (2010) 90:235–8. doi: 10.2340/00015555-0783

PubMed Abstract | CrossRef Full Text | Google Scholar

75. Ji KM, Chen JJ, Li M, Liu ZG, Wang CB, Zhan ZK, et al. Anaphylactic shock and lethal anaphylaxis caused by food consumption in China. Trends Food Sci Technol. (2009) 20:227–31. doi: 10.1016/j.tifs.2009.02.004

PubMed Abstract | CrossRef Full Text | Google Scholar

76. Ji KM, Zhan ZK, Chen JJ, Liu ZG. Anaphylactic shock caused by silkworm pupa consumption in China. Allergy. (2008) 63:1407–8. doi: 10.1111/j.1398-9995.2008.01838.x

PubMed Abstract | CrossRef Full Text | Google Scholar

77. Leung PSC, Chow WK, Duffey S, Kwan HS, Gershwin ME, Chu KH. IgE reactivity against a cross-reactive allergen in crustacea and mollusca: evidence for tropomyosin as the common allergen. J Allergy Clin Immunol. (1996) 98:954–61. doi: 10.1016/S0091-6749(96)80012-1

PubMed Abstract | CrossRef Full Text | Google Scholar

78. Jeong KY Han IS Lee JY Park KH Lee JH Park JW. Role of tropomyosin in silkworm allergy. Mol Med Report. (2017) 15:3264–70. doi: 10.3892/mmr.2017.6373

CrossRef Full Text | Google Scholar

79. Kamemura N, Sugimoto M, Tamehiro N, Adachi R, Tomonari S, Watanabe T, et al. Cross-allergenicity of crustacean and the edible insect Gryllus bimaculatus in patients with shrimp allergy. Mol Immunol. (2019) 106:127–34. doi: 10.1016/j.molimm.2018.12.015

PubMed Abstract | CrossRef Full Text | Google Scholar

80. Broekman HC, Knulst AC, Gaspari M, Jager CFD, De Jong G, Houben GF, et al. Is mealworm food allergy indicative for food allergy to other insects? Mol Nutr Food Res. (2017) 61:9. doi: 10.1002/mnfr.201601061

CrossRef Full Text | Google Scholar

81. Leung NYH, Leung ASY, Xu KJY, Wai CYY, Lam CY, Wong GWK, et al. Molecular and immunological characterization of grass carp (Ctenopharyngodon idella) parvalbumin Cten i 1: a major fish allergen in Hong Kong. Pediatr Allergy Immunol. (2020) 31:792–804. doi: 10.1111/pai.13259

PubMed Abstract | CrossRef Full Text | Google Scholar

82. Ruethers T, Raith M, Sharp MF, Koeberl M, Stephen JN, Nugraha R, et al. Characterization of Ras k 1 a novel major allergen in Indian mackerel and identification of parvalbumin as the major fish allergen in 33 Asia-Pacific fish species. Clin Exp Allergy. (2018) 48:452–63. doi: 10.1111/cea.13069

PubMed Abstract | CrossRef Full Text | Google Scholar

83. Liu R, Holck AL, Yang E, Liu C, Xue W. Tropomyosin from tilapia (Oreochromis mossambicus) as an allergen. Clin Exp Allergy. (2013) 43:365–77. doi: 10.1111/cea.12056

PubMed Abstract | CrossRef Full Text | Google Scholar

84. Kobayashi Y, Akiyama H, Huge J, Kubota H, Chikazawa S, Satoh T, et al. Fish collagen is an important panallergen in the Japanese population. Allergy. (2016) 71:720–3. doi: 10.1111/all.12836

PubMed Abstract | CrossRef Full Text | Google Scholar

85. Kalic T, Kamath SD, Ruethers T, Taki AC, Nugraha R, Le TTK, et al. Collagen-An important fish allergen for improved diagnosis. J Allergy Clin Immunol Pract. (2020) 8:3084–92. doi: 10.1016/j.jaip.2020.04.063

PubMed Abstract | CrossRef Full Text | Google Scholar

86. Yanagida N, Minoura T, Takahashi K, Sato S, Ebisawa M. Salmon roe-specific serum IgE predicts oral salmon roe food challenge test results. Pediatr Allergy Immunol. (2016) 27:324–7. doi: 10.1111/pai.12531

PubMed Abstract | CrossRef Full Text | Google Scholar

87. Liu YY, Cao MJ, Zhang ML, Hu JW, Zhang YX, Zhang LJ, et al. Purification, characterization and immunoreactivity of beta '-component, a major allergen from the roe of large yellow croaker (Pseudosciaena crocea). Food Cheml Toxicol. (2014) 72:111–21. doi: 10.1016/j.fct.2014.07.015

PubMed Abstract | CrossRef Full Text | Google Scholar

88. Makinen-Kiljunen S, Kiistala R, Varjonen E. Severe reactions from roe without concomitant rish allergy. Ann Allerg Asthma Im. (2003) 91:413–6. doi: 10.1016/S1081-1206(10)61691-2

CrossRef Full Text | Google Scholar

89. Minhas J, Saryan JA, Balekian DS. Salmon roe (ikura)-induced anaphylaxis in a child. Ann Allerg Asthma Im. (2017) 118:365–6. doi: 10.1016/j.anai.2016.11.020

PubMed Abstract | CrossRef Full Text | Google Scholar

90. Cosme J, Spinola-Santos A, Bartolome B, Pastor-Vargas C, Branco-Ferreira M, Pereira-Santos MC, et al. Salmon Roe as an emerging allergen in western countries. J Investig Allergol Clin Immunol. (2019) 29:139–41. doi: 10.18176/jiaci.0347

PubMed Abstract | CrossRef Full Text | Google Scholar

91. Perez-Gordo M, Sanchez-Garcia S, Cases B, Pastor C, Vivanco F, Cuesta-Herranz J. Identification of vitellogenin as an allergen in Beluga caviar allergy. Allergy. (2008) 63:479–80. doi: 10.1111/j.1398-9995.2007.01614.x

PubMed Abstract | CrossRef Full Text | Google Scholar

92. Reese G, Schicktanz S, Lauer I, Randow S, Luttkopf D, Vogel L, et al. Structural, immunological and functional properties of natural recombinant Pen a 1, the major allergen of Brown Shrimp, Penaeus aztecus. Clin Exp Allergy. (2006) 36:517–24. doi: 10.1111/j.1365-2222.2006.02454.x

PubMed Abstract | CrossRef Full Text | Google Scholar

93. Albrecht M, Alessandri S, Conti A, Reuter A, Lauer I, Vieths S, et al. High level expression, purification and physico- and immunochemical characterisation of recombinant Pen a 1: a major allergen of shrimp. Mol Nutr Food Res. (2008) 52:S186–95. doi: 10.1002/mnfr.200700424

PubMed Abstract | CrossRef Full Text | Google Scholar

94. Wai CYY, Leung NYH, Leung ASY, Shum Y, Leung PSC, Chu KH, et al. Cell-based functional IgE assays are superior to conventional allergy tests for shrimp allergy diagnosis. J Allergy Clin Immunol Pract. (2021) 9:236–44. doi: 10.1016/j.jaip.2020.08.057

PubMed Abstract | CrossRef Full Text | Google Scholar

95. Tsedendorj O, Chinuki Y, Ueda K, Kohno K, Adachi A, Morita E. Tropomyosin is a minor but distinct allergen in patients with shrimp allergies in Japan. J Cutan Immunol Allergy. (2018) 1:100–8. doi: 10.1002/cia2.12019

CrossRef Full Text | Google Scholar

96. Thalayasingam M, Gerez IF, Yap GC, Llanora GV, Chia IP, Chua L, et al. Clinical and immunochemical profiles of food challenge proven or anaphylactic shrimp allergy in tropical Singapore. Clin Exp Allergy. (2015) 45:687–97. doi: 10.1111/cea.12416

PubMed Abstract | CrossRef Full Text | Google Scholar

97. Wai CYY, Leung NYH, Leung ASY, Lam CY, Xu K, Shum Y, et al. IgE binding-based and cross-linking-based tests for the diagnosis of shrimp allergy. Allergy. (2019) 74:311.

Google Scholar

98. Wai CYY, Leung NYH, Leung ASY, Lam MCY, Xu K, Shum Y, et al. Troponin C is the Major Shrimp Allergen Among Chinese Patients with Shellfish Allergy. J Allergy Clin Immunol. (2019) 143:Ab270. doi: 10.1016/j.jaci.2018.12.826

CrossRef Full Text | Google Scholar

99. Khanaruksombat S, Srisomsap C, Chokchaichamnankit D, Punyarit P, Phiriyangkul P. Identification of a novel allergen from muscle and various organs in banana shrimp (Fenneropenaeus merguiensis). Ann Allerg Asthma Immunol. (2014) 113:301–6. doi: 10.1016/j.anai.2014.06.002

PubMed Abstract | CrossRef Full Text | Google Scholar

100. Park JG, Saeki H, Nakamura A, Kim KBWR, Lee JW, Byun MW, et al. Allergenicity changes in raw shrimp (Acetes japonicus) and Saeujeot (salted and fermented shrimp) in cabbage Kimchi due to fermentation conditions. Food Sci Biotechnol. (2007) 16:1011–7.

Google Scholar

101. Kim SM, Park JG, Kim KBWR, Saeki H, Nakamura A, Lee JW, et al. Changes in the allergenicity of Saeujeot by fermentation. Food Sci Biotechnol. (2008) 17:919–24.

Google Scholar

102. Suratannon N, Ngamphaiboon J, Wongpiyabovorn J, Puripokai P, Chatchatee P. Component-resolved diagnostics for the evaluation of peanut allergy in a low-prevalence area. Pediat Allerg Immunol. (2013) 24:665–70. doi: 10.1111/pai.12125

PubMed Abstract | CrossRef Full Text | Google Scholar

Keywords: prevalence, tropomyosin, parvalbumin, Crustacea, mollusk, fish

Citation: Wai CYY, Leung NYH, Leung ASY, Wong GWK and Leung TF (2021) Seafood Allergy in Asia: Geographical Specificity and Beyond. Front. Allergy 2:676903. doi: 10.3389/falgy.2021.676903

Received: 06 March 2021; Accepted: 17 June 2021;
Published: 08 July 2021.

Edited by:

Sabine Flicker, Medical University of Vienna, Austria

Reviewed by:

Ines Swoboda, University of Applied Sciences Wien, Austria
Sandip D. Kamath, James Cook University, Australia

Copyright © 2021 Wai, Leung, Leung, Wong and Leung. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

*Correspondence: Ting F. Leung, tfleung@cuhk.edu.hk

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