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Bacterial Cell Surface Structures in Yersinia enterocolitica

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Archivum Immunologiae et Therapiae Experimentalis Aims and scope

Abstract

Yersinia enterocolitica is a widespread member of the family of Enterobacteriaceae that contains both non-virulent and virulent isolates. Pathogenic Y. enterocolitica strains, especially belonging to serotypes O:3, O:5,27, O:8 and O:9 are etiologic agents of yersiniosis in animals and humans. Y. enterocolitica cell surface structures that play a significant role in virulence have been subject to many investigations. These include outer membrane (OM) glycolipids such as lipopolysaccharide (LPS) and enterobacterial common antigen (ECA) and several cell surface adhesion proteins present only in virulent Y. enterocolitica, i.e., Inv, YadA and Ail. While the yadA gene is located on the Yersinia virulence plasmid the Ail, Inv, LPS and ECA are chromosomally encoded. These structures ensure the correct architecture of the OM, provide adhesive properties as well as resistance to antimicrobial peptides and to host innate immune response mechanisms.

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References

  • Acker G (1977) The arrangement of lipopolysaccharides on the outer membrane of Yersinia enterocolitica: an electron microscopic study. Zentralbl Bakteriol Orig A 237:504–522

    PubMed  CAS  Google Scholar 

  • Acker G, Wartenberg K (1976) Ultrastructure of lipopolysaccharides of Yersinia enterocolitica, Salmonella typhimurium and Escherichia coli. Zentralbl Bakteriol Orig A 235:439–452

    PubMed  CAS  Google Scholar 

  • Acker G, Knapp W, Wartenberg K et al (1981) Localization of enterobacterial common antigen in Yersinia enterocolitica by immunoferritin technique. J Bacteriol 147:602–611

    PubMed  CAS  Google Scholar 

  • Ackermann N, Tiller M, Anding G et al (2008) Contribution of trimeric autotransporter C-terminal domains of oligomeric coiled-coil adhesin (Oca) family members YadA, UspA1, EibA, and Hia to translocation of the YadA passenger domain and virulence of Yersinia enterocolitica. J Bacteriol 190:5031–5043

    PubMed  CAS  Google Scholar 

  • Adler NRL, Govan B, Cullinane M et al (2009) The molecular and cellular basis of pathogenesis in melioidosis: how does Burkholderia pseudomallei cause disease? FEMS Microbiol Rev 33:1079–1099

    PubMed  CAS  Google Scholar 

  • Alexander C, Rietschel ET (2001) Bacterial lipopolysaccharides and innate immunity. J Endotoxin Res 7:167–202

    PubMed  CAS  Google Scholar 

  • al-Hendy A, Toivanen P, Skurnik M (1991) The effect of growth temperature on the biosynthesis of Yersinia enterocolitica O:3 lipopolysaccharide: temperature regulates the transcription of the rfb but not of the rfa region. Microb Pathog 10:81–86

    PubMed  CAS  Google Scholar 

  • al-Hendy A, Toivanen P, Skurnik M (1992) Lipopolysaccharide O side chain of Yersinia enterocolitica O:3 is an essential virulence factor in an orally infected murine model. Infect Immun 60:870–875

    PubMed  CAS  Google Scholar 

  • Aoki S, Yoshikawa K, Yokoyama T et al (1996) Role of enteric bacteria in the pathogenesis of rheumatoid arthrisis: evidence for antibodies to enterobacterial common antigens in rheumatoid sera and synovial fluids. Ann Rheum Dis 55:363–369

    PubMed  CAS  Google Scholar 

  • Aussel L, Thérisod H, Karibian D et al (2000) Novel variation of lipid A structures in strains of different Yersinia species. FEBS Lett 465:87–92

    PubMed  CAS  Google Scholar 

  • Autenrieth IB, Firsching R (1996) Penetration of M cells and destruction and destruction of Peyer’s patches by Yersinia enterocolitica: an ultrastructural and histological study. J Med Microbiol 44:285–294

    PubMed  CAS  Google Scholar 

  • Badger JL, Miller VL (1998) Expression of invasion and motility are coordinately regulated in Yersinia enterocolitica. J Bacteriol 180:793–800

    PubMed  CAS  Google Scholar 

  • Bartnik W, Kałużewski S (1979) Cellular and humoral response to Kunin antigen (CA) in ulcerative colitis and Crohn’s disease. Arch Immunol Ther Exp 27:531–538

    CAS  Google Scholar 

  • Bengoechea JA, Pinta E, Salminen T et al (2002) Functional characterization of Gne (UDP-N-acetylglucosamine-4-epimerase), Wzz (chain length determinant), and Wzy (O-antigen polymerase) of Yersinia enterocolitica serotype O:8. J Bacteriol 184:4277–4287

    PubMed  CAS  Google Scholar 

  • Bengoechea JA, Brandenburg C, Arraiza MD et al (2003) Pathogenic Yersinia enterocolitica strains increase the outer membrane permeability in response to environmental stimuli by modulating lipopolysaccharide fluidity and lipid A structure. Infect Immun 71:2014–2021

    PubMed  CAS  Google Scholar 

  • Bercovier H, Mollaret HH (1984) Genus XIV. Yersinia Van Loghem 1944. In: Krieg NR, Holt JG (eds) Bergey’s manual of systematic bacteriology. The Williams and Wilkins, Baltimore, pp 498–506

    Google Scholar 

  • Beutler B, Rietschel ET (2003) Innate immune sensing and its roots: the story of endotoxin. Nat Rev Immunol 3:169–176

    PubMed  CAS  Google Scholar 

  • Bhagat N, Virdi JS (2007) Distribution of virulence-associated genes in Yersinia enterocolitica biovar 1A correlates with clonal groups and not the source of isolation. FEMS Microbiol Lett 266:177–183

    PubMed  CAS  Google Scholar 

  • Biedzka-Sarek M, Jarva H, Hyytiäinen H et al (2008) Characterization of complement factor H binding to Yersinia enterocolitica serotype O:3. Infect Immun 76:4100–4109

    PubMed  CAS  Google Scholar 

  • Bliska JB, Falkow S (1992) Bacterial resistance to complement killing mediated by the Ail protein of Yersinia enterocolitica. Proc Natl Acad Sci USA 89:3561–3565

    PubMed  CAS  Google Scholar 

  • Bölin I, Portnoy DA, Wolf-Watz H (1985) Expression of the temperature-inducible outer membrane protein of Yersiniae. Infect Immun 48:234–240

    PubMed  Google Scholar 

  • Bottone EJ (1997) Yersinia enterocolitica: the charisma continues. Clin Microbiol Rev 10:257–276

    PubMed  CAS  Google Scholar 

  • Bottone EJ (1999) Yersinia enterocolitica: overview and epidemiologic correlates. Microbes Infect 1:323–333

    PubMed  CAS  Google Scholar 

  • Bruneteau M, Minka S (2003) Lipopolysaccharides of bacterial pathogens from the genus Yersinia: a mini-review. Biochimie 85:145–152

    PubMed  CAS  Google Scholar 

  • Caroff M, Bundle DR, Perry MB (1984) Structure of the O-chain of the phenol-phase soluble cellular lipopolysaccharide of Yersinia enterocolitica serotype O:9. Eur J Biochem 139:195–200

    PubMed  CAS  Google Scholar 

  • Chart H, Row B, Threlfall EJ et al (1989) Conversion of Salmonella enteritidis phage type 4 to phage type 7 involves loss of lipopolysaccharide with concomitant loss of virulence. FEMS Microbiol Lett 51:37–40

    PubMed  CAS  Google Scholar 

  • Cotter SE, Surana NK, Geme JW 3rd (2005) Trimeric autotransporters: a distinct subfamily of autotransporter proteins. Trends Microbiol 13:199–205

    PubMed  CAS  Google Scholar 

  • de Rouvroit CLL, Sluiters C, Cornelis GR (1992) Role of the transcriptional activator, VirF, and temperature in the expression of the pYV plasmid genes of Yersinia enterocolitica. Mol Microbiol 6:395–409

    Google Scholar 

  • Deuretzbacher A, Czymmeck N, Reimer R et al (2009) β1 integrin-dependent engulfment of Yersinia enterocolitica by macrophages is coupled to the activation of autophagy and suppressed by type III protein secretion. J Immunol 183:5847–5860

    PubMed  CAS  Google Scholar 

  • Diaz F, Neter E (1968) Antibody response to the common enterobacterial antigen of children with shigellosis, salmonellosis or urinary tract infections. Am J Med Sci 256:18–24

    PubMed  CAS  Google Scholar 

  • Diaz R, Urra E, Toyos J et al (1985) Characterization of a Yersinia enterocolitica antigen common to enterocolitis-associated serotypes. J Clin Microbiol 22:1035–1039

    PubMed  CAS  Google Scholar 

  • Dube PH, Handley SA, Revell PA et al (2003) The rovA mutant of Yersinia enterocolitica displays differential degrees of virulence depending on the route of infection. Infect Immun 71:3512–3520

    PubMed  CAS  Google Scholar 

  • Duda KA, Duda KT, Beczała A et al (2009) ECA-immunogenicity of Proteus mirabilis strains. Arch Immunol Ther Exp 57:147–151

    CAS  Google Scholar 

  • El Tahir Y, Skurnik M (2001) YadA, the multifaceted Yersinia adhesin. Int J Med Microbiol 291:209–218

    PubMed  Google Scholar 

  • Erridge C, Bennett-Guerrero E, Poxton IR (2002) Structure and function of lipopolysaccharides. Microbes Infect 4:837–851

    PubMed  CAS  Google Scholar 

  • Frederiksen W (1964) A study of some Yersinia pseudotuberculosis-like bacteria (“Bacterium enterocoliticum” and Pasteurella X). In: Proceedings of the 14th Scandinavian Congress on pathology and microbiology, Norway, pp 103–104

  • Fredriksson-Ahomaa M (2001) Molecular epidemiology of yadA-positive Yersinia enterocolitica. Academic dissertation, Helsinki, p 22

    Google Scholar 

  • Gorshkova RP, Kalmykova EN, Isakov VV et al (1985) Structural studies on O-specific polysaccharide of lipopolysaccharide from Yersinia enterocolitica serovars O:1,2a,3, O:2a,2b,3 and O:3. Eur J Biochem 150:527–531

    PubMed  CAS  Google Scholar 

  • Gromska W, Izdebska-Szymona K (1987) Antygen Kunina (ECA). Postepy Hig Med Dośw 41:512–532

    PubMed  CAS  Google Scholar 

  • Henderson IR, Navarro-Garcia F, Desvaux M et al (2004) Type V protein secretion pathway: the autotransporter story. Microbiol Mol Biol Rev 68:692–744

    PubMed  CAS  Google Scholar 

  • Hoffman J, Lindberg B, Brubakev RR (1980) Structural studies of the O-specific side-chains of the lipopolysaccharide from Yersinia enterocolitica Ye 128. Carbohydr Res 78:212–214

    PubMed  CAS  Google Scholar 

  • Hoiczyk E, Roggenkamp A, Reichenbecher M et al (2000) Structure and sequence analysis of Yersinia YadA and Moraxella UspAs reveal a novel class of adhesions. EMBO J 19:5989–5999

    PubMed  CAS  Google Scholar 

  • Holst O (2007) The structures of core regions from enterobacterial lipopolysaccharides: an update. FEMS Microbiol Lett 271:3–11

    PubMed  CAS  Google Scholar 

  • Hudson JA, King NJ, Cornelius AJ et al (2008) Detection, isolation and enumeration of Yersinia enterocolitica from raw pork. Int J Food Microbiol 123:25–31

    PubMed  CAS  Google Scholar 

  • Hurst MR, Becher SA, Young SD et al (2011) Yersinia entomophaga sp. nov. isolated from the New Zealand grass grub Costelytra zealandica. Int J Sys Evol Microbiol 61:844–849

    CAS  Google Scholar 

  • Iriarte M, Cornelis GR (1995) MyfF, an element of the network regulating the synthesis of fibrillae in Yersinia enterocolitica. J Bacteriol 177:738–744

    PubMed  CAS  Google Scholar 

  • Iriarte M, Vanooteghem JC, Delor I et al (1993) The Myf fibrillae of Yersinia enterocolitica. Mol Microbiol 9:507–520

    PubMed  CAS  Google Scholar 

  • Isberg RR, Leong JM (1990) Multiple B1 chain integrins are receptors for invasin a protein that promotes bacterial penetration into mammalian cells. Cell 60:861–871

    PubMed  CAS  Google Scholar 

  • Jepson MA, Clark MA (1998) M cells and their role in infection. Trends Microbiol 6:359–365

    PubMed  CAS  Google Scholar 

  • Journet L, Agrain C, Broz P et al (2003) The needle length of bacterial injectisomes is determined by a molecular ruler. Science 302:1757–1760

    PubMed  CAS  Google Scholar 

  • Kajimura J, Rahman A, Rick PD (2005) Assembly of cyclic enterobacterial common antigen in Escherichia coli K-12. J Bacteriol 187:6917–6927

    PubMed  CAS  Google Scholar 

  • Kajimura J, Rahman A, Hsu J et al (2006) O-acetylation of the enterobacterial common antigen polysaccharide is catalyzed by the product of the yiaH gene of Escherichia coli K-12. J Bacteriol 188:7542–7550

    PubMed  CAS  Google Scholar 

  • Kałużewski S (1974) Przeciwciała dla antygenu wspólnego pałeczkom Enterobacteriaceae (CA Kunina) w surowicach ludzkich. Med Dośw Mikrobiol 26:27–43

    Google Scholar 

  • Karabian D, Brunelle A, Aussel L et al (1999) 252Cf-plasma desorption mass spectrometry of unmodified lipid A: fragmentation patterns and localization of fatty acids. Rapid Commun Mass Spectrom 13:2252–2259

    Google Scholar 

  • Kasperkiewicz K, Skurnik M, Brade L (2004) Monoclonal antibodies specific for lipid A and ECA as tools in characterization of lipopolysaccharides from enterobacterial R mutants. In: 3rd German–Polish–Russian meeting on bacterial carbohydrates, October 6–9, Wrocław, Poland. Abstract P10

  • Kawaoka Y, Otsuki K, Tsubokura M (1983) Growth temperature-dependent variation in the bacteriophage-inactivating capacity and antigenicity of Yersinia enterocolitica lipopolysaccharide. J Gen Microbiol 129:2739–2747

    PubMed  CAS  Google Scholar 

  • Keck M, Gisch N, Moll H et al (2011) Unusual outer membrane lipid composition of the Gram-negative, lipopolysaccharide-lacking Myxobacterium Sorangium cellulosum So ce56. J Biol Chem 286:12850–12859

    PubMed  CAS  Google Scholar 

  • Kenne L, Lindberg B (1983) Bacterial polysaccharides. In: Aspinall GO (ed) Molecular biology: the polysaccharides. Academic Press, New York, pp 287–365

    Google Scholar 

  • Kirjavainen V, Jarva H, Biedzka-Sarek M et al (2008) Yersinia enterocolitica serum resistance proteins YadA and Ail bind the complement regulator C4b-binding protein. PLoS Pathog 4:e1000140

    PubMed  Google Scholar 

  • Knirel YA, Kochetkov NK (1994) The structure of lipopolysaccharides of Gram-negative bacteria. III. The structure of O-antigens. Biokhimiia 59:1784–1851

    PubMed  CAS  Google Scholar 

  • Koretke KK, Szczesny P, Gruber M et al (2006) Model structure of the prototypical non-fimbrial adhesin YadA of Yersinia enterocolitica. J Struct Biol 155:154–161

    PubMed  CAS  Google Scholar 

  • Kuhn HM, Meier-Dieter U, Mayer H (1988) ECA, the enterobacterial common antigen. FEMS Microbiol Rev 4:195–222

    PubMed  CAS  Google Scholar 

  • Kunin CM, Beard MV, Halmagyi NE (1962) Evidence for a common hapten associated with endotoxin fractions of E. coli and other Enterobacteriaceae. Proc Soc Exp Biol Med 111:160–166

    CAS  Google Scholar 

  • Lachica RV, Zink DL (1984) Plasmid-associated cell surface charge and hydrophobicity of Yersinia enterocolitica. Infect Immun 44:540–543

    PubMed  CAS  Google Scholar 

  • Loppnow H, Brade H, Dürrbaum I et al (1989) IL-1 induction-capacity of defined lipopolysaccharide partial structures. J Immunol 142:3229–3238

    PubMed  CAS  Google Scholar 

  • Lüderitz O, Freudenberg MA, Galanos C et al (1982) Lipopolysaccharides of Gram-negative bacteria. Curr Top Membr Transp 17:79–151

    Google Scholar 

  • Malkamäki M (1981) Antibodies to the enterobacterial common antigen: standardization of the passive hemagglutination test and levels in normal human sera. J Clin Microbiol 13:1074–1079

    PubMed  Google Scholar 

  • Marceau M (2005) Transcriptional regulation in Yersinia: an update. Curr Issues Mol Biol 7:151–177

    PubMed  CAS  Google Scholar 

  • Mayer H, Schmidt G (1979) Chemistry and biology of the enterobacterial common antigen (ECA). Curr Top Microbiol Immunol 85:99–153

    PubMed  CAS  Google Scholar 

  • McIver MA, Pike RM (1934) Chronic glanders-like infection of face caused by an organism resembling Flavobacterium pseudomallei Whitmore. In: Clinical miscellany, vol 1. Mary Imogene Basset Hospital, Cooperstown, New York, pp 16–21

  • Medzhitov R, Janeway CA Jr (2000) Innate immunity. N Engl J Med 343:338–344

    PubMed  CAS  Google Scholar 

  • Merhej V, Adekambi T, Pagnier I et al (2008) Yersinia massiliensis sp. nov., isolated from fresh water. Int J Syst Evol Microbiol 58(Pt 4):779–784

    PubMed  Google Scholar 

  • Miller VL, Beer KB, Heusipp G et al (2001) Identification of regions of Ail required for the invasion and serum resistance phenotypes. Mol Microbiol 41:1053–1062

    PubMed  CAS  Google Scholar 

  • Müller-Loennies S, Rund S, Ervelä E et al (1999) The structure of the carbohydrate backbone of the core-lipid A region of the lipopolysaccharide from a clinical isolate of Yersinia enterocolitica O:9. Eur J Biochem 261:19–24

    PubMed  Google Scholar 

  • Murros-Kontiainen AE, Fredriksson-Ahomaa M, Korkeala H et al (2011a) Yersinia nurmii sp. nov. Int J Syst Evol Microbiol 61(Pt 10):2368–2372

    PubMed  Google Scholar 

  • Murros-Kontiainen AE, Johansson P, Niskanen T et al (2011b) Yersinia pekkanenii sp. nov. Int J Syst Evol Microbiol 61(Pt 10):2363–2367

    PubMed  CAS  Google Scholar 

  • Nummelin H, Merckel MC, Leo JC et al (2004) The Yersinia adhesin YadA collagen-binding domain structure is a novel left-handed parallel beta-roll. EMBO J 23:701–711

    PubMed  CAS  Google Scholar 

  • Oertelt C, Lindner B, Skurnik M et al (2001) Isolation and structural characterization of an R-form lipopolysaccharide from Yersinia enterocolitica serotype O:8. Eur J Biochem 268:554–564

    PubMed  CAS  Google Scholar 

  • Parrillo JE (1993) Pathogenic mechanisms of septic shock. N Engl J Med 328:1471–1478

    PubMed  CAS  Google Scholar 

  • Pederson KJ, Pierson DE (1995) Ail expression in Yersinia enterocolitica is affected by oxygen tension. Infect Immun 63:4199–4201

    PubMed  CAS  Google Scholar 

  • Pepe JC, Miller VL (1993) Yersinia enterocolitica invasin: a primary role in the initiation of infection. Proc Natl Acad Sci USA 90:6473–6477

    PubMed  CAS  Google Scholar 

  • Pepe JC, Badger JL, Miller VL (1994) Growth phase and low pH affect the thermal regulation of the Yersinia enterocolitica inv gene. Mol Microbiol 11:123–135

    PubMed  CAS  Google Scholar 

  • Perez-Gutierrez C, Llobet E, Llompart CM et al (2010) Role of lipid A acylation on Y. enterocolitica virulence. Infect Immun 78:2768–2781

    PubMed  CAS  Google Scholar 

  • Persing DH, Coler RN, Lacy MJ et al (2002) Taking toll: lipid A mimetics as adjuvants and immunomodulators. Trends Microbiol 10(10 suppl):S32–S37

    PubMed  CAS  Google Scholar 

  • Pinta E, Duda KA, Hanuszkiewicz A et al (2009) Identification and role of a 6-deoxy-4-keto-hexosamine in the lipopolysaccharide outer core of Yersinia enterocolitica serotype O:3. Chemistry 15:9747–9754

    PubMed  CAS  Google Scholar 

  • Pinta E, Duda KA, Hanuszkiewicz A et al (2010) Characterization of the six glycosyltransferases involved in the biosynthesis of Yersinia enterocolitica serotype O:3 lipopolysaccharide outer core. J Biol Chem 285:28333–28342

    PubMed  CAS  Google Scholar 

  • Portnoy DA, Wolf-Watz H, Bölin I et al (1984) Characterization of common virulence plasmids in Yersinia species and their role in the expression of outer membrane proteins. Infect Immun 43:108–114

    PubMed  CAS  Google Scholar 

  • Rabsztyn K, Kasperkiewicz K, Duda KA et al (2011) Characterization of anti-ECA antibodies in rabbit antiserum against rough Yersinia enterocolitica O:3. Biochemistry 76:832–839

    PubMed  CAS  Google Scholar 

  • Radziejewska-Lebrecht J, Shashkov AS, Stroobant V et al (1994) The inner core region of Yersinia enterocolitica Ye75R (0:3) lipopolysaccharide. Eur J Biochem 221:343–351

    PubMed  CAS  Google Scholar 

  • Radziejewska-Lebrecht J, Skurnik M, Shashkov AS et al (1998) Studies on R-mutants of Yersinia enterocolitica O:3. Acta Biochim Pol 45:1011–1019

    PubMed  CAS  Google Scholar 

  • Radziejewska-Lebrecht J, Kasperkiewicz K, Skurnik M (2003) ECA-antibodies in antisera against R mutants of Yersinia enterocolitica O:3. Adv Exp Med Biol 529:215–218

    PubMed  Google Scholar 

  • Revell PA, Miller VL (2000) A chromosomally encoded regulator is required for expression of the Yersinia enterocolitica inv gene and for virulence. Mol Microbiol 35:677–685

    PubMed  CAS  Google Scholar 

  • Rietschel ET, Kirikae T, Feist W et al (1991) Molecular aspects of the chemistry and biology of endotoxin. In: Zimmer G (ed) Molecular aspects of inflammation. Springer, Berlin, pp 207–231

    Google Scholar 

  • Rietschel ET, Kirikae T, Schade FU et al (1994) Bacterial endotoxin: molecular relationships of structure to activity and function. FASEB J 8:217–225

    PubMed  CAS  Google Scholar 

  • Roggenkamp A, Ackermann N, Jacobi CA et al (2003) Molecular analysis of transport and oligomerization of the Yersinia enterocolitica adhesin YadA. J Bacteriol 185:3735–3744

    PubMed  CAS  Google Scholar 

  • Schleifstein JI, Coleman MB (1939) An unidentified microorganism resembling B. lignieri and Past. pseudotuberculosis and pathogenic for man. NY State J Med 39:1749–1753

    Google Scholar 

  • Schleifstein JI, Coleman MB (1943) Bacterium enterocoliticum. Ann Rep Division of Laboratories and Research, New York Department of Health, Albany, p 56

    Google Scholar 

  • Schulze-Koops H, Burkhardt H, Heesemann J et al (1992) Plasmid-encoded outer membrane protein YadA mediates specific binding of enteropathogenic yersiniae to various types of collagen. Infect Immun 60:2153–2159

    PubMed  CAS  Google Scholar 

  • Schulze-Koops H, Burkhardt H, Heesemann J et al (1993) Outer membrane protein YadA of enteropathogenic yersiniae mediates specific binding to cellular but not plasma fibronectin. Infect Immun 61:2513–2519

    PubMed  CAS  Google Scholar 

  • Seltmann G, Holst O (2002) The bacterial cell wall. Springer, Berlin, pp 31–102

    Google Scholar 

  • Seydel U, Wiese A, Schromm AB et al (1999) A biophysical view on the function and activity of endotoxins. In: Brade H, Opal SM, Vogel SN et al (eds) Endotoxin in health and disease. Marcel Dekker, New York, pp 195–219

    Google Scholar 

  • Silhavy JT, Kahne D, Walker S (2010) The bacterial cell envelope. Cold Spring Harb Perspect Biol 2:a000414

    PubMed  Google Scholar 

  • Skurnik M, Wolf-Watz H (1989) Analysis of the yopA gene encoding the Yop1 virulence determinants of Yersinia spp. Mol Microbiol 3:517–529

    PubMed  CAS  Google Scholar 

  • Skurnik M, Bölin I, Heikkinen H et al (1984) Virulence plasmid-associated autoagglutination in Yersinia spp. J Bacteriol 158:1033–1036

    PubMed  CAS  Google Scholar 

  • Skurnik M, Venho R, Toivanen P et al (1995) A novel locus of Yersinia enterocolitica serotype O:3 involved in lipopolysaccharide outer core biosynthesis. Mol Microbiol 17:575–594

    PubMed  CAS  Google Scholar 

  • Skurnik M, Venho R, Bengoechea JA et al (1999) The lipopolysaccharide outer core of Yersinia enterocolitica serotype O:3 is required for virulence and plays a role in outer membrane integrity. Mol Microbiol 31:1443–1462

    PubMed  CAS  Google Scholar 

  • Sprague LD, Neubauer H (2005) Yersinia aleksiciae sp. nov. Int J Syst Evol Microbiol 55(Pt 2):831–835

    PubMed  CAS  Google Scholar 

  • Sprague LD, Scholz HC, Amann S et al (2008) Yersinia similis sp. nov. Int J Syst Evol Microbiol 58(Pt 4):952–958

    PubMed  CAS  Google Scholar 

  • Sulakvelidze A (2000) Yersiniae other than Y. enterocolitica, Y. pseudotuberculosis, and Y. pestis, the ignored species. Microbes Infect 2:497–513

    PubMed  CAS  Google Scholar 

  • Swain P, Nayak SK, Nanda PK et al (2008) Biological effects of bacterial lipopolysaccharide (endotoxin) in fish: a review. Fish Shellfish Immunol 25:191–201

    PubMed  CAS  Google Scholar 

  • Tomshich SV, Gorshkova RP, Ovodov YS (1987) Structural investigations of the lipopolysaccharide of Yersinia enterocolitica serovar O:8. Khim Prirod Soed 5:657–664

    Google Scholar 

  • Uliczka F, Pisano F, Schaake J et al (2011) Unique cell adhesion and invasion properties of Yersinia enterocolitica O:3, the most frequent cause of human yersiniosis. PLoS Pathog 7:e1002117

    PubMed  CAS  Google Scholar 

  • Valtonen MV, Larinkari UM, Plosila M et al (1976) Effect of enterobacterial common antigen on mouse virulence of Salmonella typhimurium. Infect Immun 13:1601–1605

    PubMed  CAS  Google Scholar 

  • Van Loghem JJ (1944–1945) The classification of plague-bacillus. Antonie Van Leeuwenhoek 10:15

  • Virdi JS, Sachdeva P (2005) Molecular heterogeneity in Yersinia enterocolitica and ‘Y. enterocolitica-like’ species: implications for epidemiology, typing and taxonomy. FEMS Immunol Med Microbiol 45:1–10

    PubMed  CAS  Google Scholar 

  • Wang X, Quinn PJ (2010) Lipopolysaccharide: biosynthetic pathway and structure modification. Prog Lipid Res 49:97–107

    PubMed  CAS  Google Scholar 

  • Wang X, Ribeiro AA, Guan Z et al (2006) Structure and biosynthesis of free lipid A molecules that replace lipopolysaccharide in Francisella tularensis subsp Novicida. Biochemistry 45:14427–14440

    PubMed  CAS  Google Scholar 

  • Wartenberg K, Knapp W, Ahamed NM et al (1983) Temperature-dependent changes in the sugar and fatty acid composition of lipopolysaccharide from Yersinia enterocolitica strains. Zentralbl Bakteriol Microbiol Hyg A 253:523–530

    CAS  Google Scholar 

  • Whang HY, Mayer H, Schmidt G et al (1972) Immunogenicity of the common enterobacterial antigen produced by smooth and rough stains. Infect Immun 6:533–539

    PubMed  CAS  Google Scholar 

  • Zaleska M, Lounatmaa K, Nurminen M et al (1985) A novel virulence-associated cell surface structure composed of 47-kd protein subunits in Yersinia enterocolitica. EMBO J 4:1013–1018

    PubMed  CAS  Google Scholar 

  • Zhang L, Radziejewska-Lebrecht J, Krajewska-Pietrasik D et al (1997) Molecular and chemical characterization of the lipopolysaccharide O-antigen and its role in the virulence of Yersinia enterocolitica serotype O:8. Mol Microbiol 23:63–76

    PubMed  CAS  Google Scholar 

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Authors and Affiliations

  1. Department of Microbiology, Faculty of Biology and Environmental Protection, University of Silesia, Katowice, Poland

    Nataniel Białas, Katarzyna Kasperkiewicz & Joanna Radziejewska-Lebrecht

  2. Department of Bacteriology and Immunology, Haartman Institute, University of Helsinki, PO Box 21, Haartmaninkatu 3, 00014, Helsinki, Finland

    Mikael Skurnik

  3. Helsinki University Central Hospital Laboratory Diagnostics, Helsinki, Finland

    Mikael Skurnik

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  1. Nataniel Białas
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  3. Joanna Radziejewska-Lebrecht
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  4. Mikael Skurnik
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Correspondence to Mikael Skurnik.

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Białas, N., Kasperkiewicz, K., Radziejewska-Lebrecht, J. et al. Bacterial Cell Surface Structures in Yersinia enterocolitica . Arch. Immunol. Ther. Exp. 60, 199–209 (2012). https://doi.org/10.1007/s00005-012-0168-z

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  • DOI: https://doi.org/10.1007/s00005-012-0168-z

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