Antifungal and antibacterial activities of lectin from the seeds of Archidendron jiringa Nielsen
Research highlights
► Many plants contain proteins that are usually referred to as lectins on the basis of their specific carbohydrate-binding properties. ► They were originally only isolated from plant extracts and were used for the agglutination of blood cells. ► Some of the lectins isolated from plants were found to exhibit different biological activities. ► This paper reports on the inhibitory effect of purified A. jiringa seed lectin against growth of plant-pathogenic bacteria and fungi.
Introduction
Lectins are proteins or glycoproteins of a ubiquitous distribution in nature, which have at least one carbohydrate or derivative binding site without catalytic function or immunological characteristics. They have the unique ability to recognise and bind reversibly to specific carbohydrate ligands without any chemical modification; this distinguishes lectins from other carbohydrate binding proteins and enzymes, and makes them invaluable tools in biomedical and glycoconjugate research (Peumans & Van Damme, 1995). Plants were the first discovered source of lectins and, although lectins have since been found to be universally distributed, plants remain the most frequently used source of lectin studies due to both the ease of their extraction and the relatively high yields that can be obtained. Moreover, different families of plants, as well as different tissues within the same plant, can contain different lectins with different bioactivities, including different carbohydrate-binding specificities. It has been suggested that plant lectins may have important roles according to their abundance, including in the immune defence, and also that lectins have been co-opted adapted for several functions during evolution (Sharon & Lis, 2001).
The role of lectins in the defense mechanism of plants may have evolved from the ability to lectins to agglutinate and immobilise microorganisms. The supporting evidence for this proposed role in defense against pathogens falls into two main observed categories, namely (a) the presence of lectins at potential sites of invasion by infectious agents, and (b) the binding of lectins to various fungi and their ability to inhibit fungal growth and germination. A number of studies with respect to the potential defense role of plant lectins have been reported. For example, during the imbibition of dry soybean seeds, lectin is released into the water and the presence of this lectin in the vicinity of germinating seeds hints at possible interactions of lectins with potential pathogens. The developmental pattern of the initial accumulation and final disappearance of lectin can be observed during the seed dormancy, germination and maturation, which may implicate the role of lectins in a defense mechanism necessary for plants in the initial stages of growth. Moreover, some lectins may provide some protection to plants against generalist herbivores (Howard et al., 1972, Peumans and Van Damme, 1995).
Archidendron jiringa Nielsen (Fabaceae: Mimosoideae), the Jenkol bean or Luk Nieng tree, is a leguminous tree that is found in Indonesia, Malaysia and Thailand, and is economically important with diverse uses, including as a vegetable (young shoots) and pulse or food flavouring agent (seeds), medicine (leaves), source of dye for silk (pods) and timber for craft work and firewood (Ong & Norzalina, 1999). Given the abundance of this commercial species, and especially the abundant seed production (1000–4000 seeds per tree per year).
An overwhelming number of plant lectins have been isolated and characterised from various diverse plant families. The majority of the well characterised plant lectins have been isolated from the seeds of plants, such as Leguminoseae. However, plant lectins of seeds from other plant species outside of legumes (mimosaceous plants) are also emerging as promising tools, chiefly because they can contain novel sugar binding sites and can provide valuable information regarding the biological roles of plant lectins, which to a large extent still remains elusive. The objective of this research was to evaluate an appropriate isolation and purification technique for lectin(s) from the abundantly produced A. jiringa seeds and to biochemically characterise the lectin obtained for future novel applications.
Section snippets
Biological material
Seeds of A. jiringa were purchased from a local market (Bangkok, Thailand). A voucher specimen (BKF. No. 8261) is deposited at The Forest Herbarium (BKF), Royal Forest Department, Bangkok, Thailand. The human blood was obtained from the blood donation office of the Thai Red Cross Society, Bangkok, Thailand. All other animal blood was supplied from the Division of Production and Supply, National Laboratory Animal Center, Mahidol University, Nakhon Pathom, Thailand. The five bacterial strains
Purification of lectin from the seeds of A. jiringa
The present report represents the first investigation on the purification of a lectin from A. jiringa seeds. A. jiringa seeds were homogenated and defated to form a crude soluble extract and, after 90% saturation ammonium sulphate precipitation and dialysis, the lectin was purified in a single step by affinity chromatography column using ConA Sepharose, yielding a single apparent lectin at ∼3.3% (w/w) of the total starting seed weight. The yield and specific agglutination activity, as a marker
Conclusions
A lectin was purified from the seeds of A. jiringa by ConA Sepharose based affinity chromatography with elution by competitive displacement using methyl-α-d-glucopyranoside. The hemagglutination activity of lectin was optimal at pH 8 and relatively stabile, although suboptimal, at acidic pH values down to pH 2, but was markedly reduced by more basic pH values above 8. The lectin was heat stable below 45 °C for 30 min, with 50% of its maximum activity being retained after 120 min of incubation at 40
Acknowledgements
The authors wish to thank the Chulalongkorn University graduate school thesis grant, the National Research University Project of CHE, the Ratchadaphiseksomphot Endowment Fund (AM007I), and the Thai Government Stimulus Package 2 (TKK2555), for financial support of this research, as well as the Institute of Biotechnology and Genetic Engineering and Biotechnology program, the Faculty of Science, Chulalongkorn University for support and facilities. We also wish to thank Dr. Robert Butcher
References (31)
- et al.
Legume lectins interact with muramic acid and N-acetylmuramic acid
FEBS Letters
(1991) A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding
Analytical Biochemistry
(1976)- et al.
Fusarium sp. growth inhibition by wheat germ agglutinin
Biochimica et Biophysica Acta (BBA)-General Subjects
(1999) - et al.
Isolation and partial characterization of a novel lectin from Talisia esculenta seeds that interferes with fungal growth
Plant Physiology and Biochemistry
(2002) - et al.
Studies on the appearance and location of hemagglutinins from a common lentil during the life cycle of the plant
Archives of Biochemistry and Biophysics
(1972) - et al.
Isolation of an N-acetyl-D-glucosamine specific lectin from the rhizomes of Arundo donax with antiproliferative activity
Phytochemistry
(2005) - et al.
Isolation and partial characterisation of galactose-specific lectins from African yam beans, Sphenostyles stenocarpa Harms
Phytochemistry
(1999) - et al.
Malay Herbal Medicine in Gemenceh, Negri Sembilan, Malaysia
Fitoterapia
(1999) - et al.
Purification and biological effects of Araucaria angustifolia (Araucariaceae) seed lectin
Biochemical and Biophysical Research Communications
(2006) - et al.
Isolation and characterization of a lectin with antifungal activity from Egyptian Pisum sativum seeds
Food Chemistry
(2007)
Isolation and characterisation of a Salvia bogotensis seed lectin specific for the Tn antigen
Phytochemistry
1H-NMR Study of the interaction of N, N′, N′′-triacetyl chitotriose with Ac-Amp2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus
FEBS Letters
Crystal structure of native and Cd/Cd-substituted Dioclea guianensis seed lectin. A novel manganese-binding site and structural basis of dimer-tetramer association
Journal of Molecular Biology
A mannose/glucose-specific lectin from Chinese evergreen chinkapin (Castanopsis chinensis)
Biochimica et Biophysica Acta (BBA)-General Subjects
Single step purification, characterization and N-terminal sequences of a mannose specific lectin from mulberry seeds
Protein Journal
Cited by (78)
Plant lectins: A New Antimicrobial Frontier
2022, Biomedicine and PharmacotherapyCitation Excerpt :These results indicate that the oligomeric association is essential for the toxic properties of the lectin [111]. For more lectins with antifungal properties, please refer to [53,112–121] and Table 2. Lectins are peculiar versatile carbohydrate-binding proteins.
Antibacterial, antifungal and in vivo anticancer activities of chitin-binding lectins from Tomato (Solanum lycopersicum) fruits
2022, Arabian Journal of Chemistry