Skip to main content
SpringerLink
Log in

Fimbrial Polyadhesins: Anti-immune Armament of Yersinia

  • Conference paper
  • First Online:
Advances in Yersinia Research

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 954))

Abstract

The adhesive organelles play a pivotal role in the initiation of bacterial infections. The 3D structure of adhesin subunits bound to host-cell receptors and the final architecture of the fimbrial adhesive organelles of Gram-negative pathogens reveal two functional families of the organelles, respectively, possessing polyadhesive and monoadhesive binding. The F1, pH6 (Psa), and Myf antigens of Yersinia are the typical members of FGL (having a long F1–G1 loop) chaperone-assembled polyadhesins belonged to the γ3-monophyletic group. High-resolution structures of the F1 minifibers confirm that Yersinia pestis capsule is made of linearly polymerized Caf1 subunits and exploit the principle of donor-strand complementation for their polymerization. The F1 and pH6 polyadhesins contribute to the powerful anti-immune armament of Y. pestis and act in concert with the Yersinia type III secretion injectisome. The binding of F1 and pH6 polyadhesins to the specific host-cell receptors may lead to their massive aggregation that triggers suicidal proinflammatory responses.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 169.00
Price excludes VAT (USA)
  • Available as EPUB and PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 219.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

References

  • Anderson KL, Billington J, Pettigrew D (2004a) An atomic resolution model for assembly, architecture, and function of the Dr adhesins. Mol Cell 101:647–657

    Article  Google Scholar 

  • Anderson KL, Cota E, Simpson P et al (2004b) Complete resonance assignments of a ‘donor-strand complemented’ AfaE: the afimbrial adhesin from diffusely adherent E. coli. J Biomol NMR 29:409–410

    Article  PubMed  CAS  Google Scholar 

  • Anisimov AP, Bakhteeva IV, Panfertsev EA et al (2009) The subcutaneous inoculation of pH 6 antigen mutants of Yersinia pestis does not affect virulence and immune response in mice. J Med Microbiol 58:26–36

    Article  PubMed  CAS  Google Scholar 

  • Ben-Efraim S, Aronson M, Bichowsky-Slomnicki L (1961) New antigenic component of Pasteurella pestis formed under specific conditions of pH and temperature. J Bacteriol 81:704–714

    PubMed  CAS  Google Scholar 

  • Bork P, Holm L, Sander C (1994) The immunoglobulin fold: structural classification, sequence patterns and common core. J Mol Biol 242:309–320

    PubMed  CAS  Google Scholar 

  • Cathelyn JS, Crosby SD, Lathem WW et al (2006) RovA, a global regulator of Yersinia pestis, specifically required for bubonic plague. Proc Natl Acad Sci U S A 103:13514–13519

    Article  PubMed  CAS  Google Scholar 

  • Chen TH, Elberg SS (1977) Scanning electron microscopic study of virulent Yersinia pestis and Yersinia pseudotuberculosis type 1. Infect Immun 15:972–977

    PubMed  CAS  Google Scholar 

  • Choudhury D, Thompson A, Stojanoff V et al (1999) X-ray structure of the FimC-FimH chaperone–adhesin complex from uropathogenic Escherichia coli. Science 285:1061–1066

    Article  PubMed  CAS  Google Scholar 

  • Cleri DJ, Vernaleo JR, Lombardi LJ et al (1997) Plague pneumonia disease caused by Yersinia pestis. Semin Respir Infect 12:12–23

    PubMed  CAS  Google Scholar 

  • Cornelis GR (2010) The type III secretion injectisome, a complex nanomachine for intracellular ‘toxin’ delivery. Biol Chem 391:745–751

    Article  PubMed  CAS  Google Scholar 

  • Cornelis GR, Wolf-Watz H (1997) The Yersinia Yop virulon: a bacterial system for subverting eukaryotic cells. Mol Microbiol 23:861–867

    Article  PubMed  CAS  Google Scholar 

  • Cota E, Chen HA, Anderson KL et al (2004) Letter to the editor: complete resonance assignments of the ‘donor-strand complemented’ AfaD: the afimbrial invasin from diffusely adherent E. coli. J Biomol NMR 29:411–412

    Article  PubMed  CAS  Google Scholar 

  • Cota E, Jones C, Simpson P et al (2006) The solution structure of the invasive tip complex from Afa/Dr fibrils. Mol Microbiol 62:356–366

    Article  PubMed  CAS  Google Scholar 

  • De Jong B, Ekdahl B (2006) The comparative burden of salmonellosis in the European Union member states, associated and candidate countries. BMC Public Health 6:4

    Article  PubMed  Google Scholar 

  • Deisenhofer J (1981) Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-Å resolution. Biochemistry 20:2361–2370

    Article  PubMed  CAS  Google Scholar 

  • DeLano WL (2002) Unraveling hot spots in binding interfaces: progress and challenges. Curr Opin Struct Biol 12:14–20

    Article  PubMed  CAS  Google Scholar 

  • Diepold A, Amstutz M, Abel S et al (2010) Deciphering the assembly of the Yersinia type III secretion injectisome. EMBO J 29:1928–1940

    Article  PubMed  CAS  Google Scholar 

  • Du Y, Rosqvist R, Forsberg Å (2002) Role of fraction 1 antigen of Yersinia pestis in inhibition of phagocytosis. Infect Immun 70:1453–1460

    Article  PubMed  CAS  Google Scholar 

  • Dutt AK, Akhtar R, McVeigh M (2006) Surat plague of 1994 reexamined. Southeast Asian J Trop Med Public Health 37:755–760

    PubMed  Google Scholar 

  • Felek S, Tsang TM, Krukonis ES (2010) Three Yersinia pestis adhesins facilitate Yop delivery to eukaryotic cells and contribute to plague virulence. Infect Immun 78:4134–4150

    Article  PubMed  CAS  Google Scholar 

  • Fronzes R, Remaut H, Waksman G (2008) Architectures and biogenesis of non-flagellar protein appendages in Gram-negative bacteria. EMBO J 27:2271–2280

    Article  PubMed  CAS  Google Scholar 

  • Galván EM, Chen H, Schifferli DM (2006) The Psa fimbriae of Yersinia pestis interact with phosphatidylcholine on alveolar epithelial cells and pulmonary surfactant. Infect Immun 75:1272–1279

    Article  PubMed  Google Scholar 

  • Galván EM, Nair MK, Chen H et al (2010) Biosafety level 2 model of pneumonic plague and protection studies with F1 and Psa. Infect Immun 78:3443–3453

    Article  PubMed  Google Scholar 

  • Galyov EE, Smirnov OY, Karlyshev AV et al (1990) Nucleotide sequence of the Yersinia pestis gene encoding F1 antigen and the primary structure of the protein. FEBS Lett 277:230–232

    Article  PubMed  CAS  Google Scholar 

  • Galyov EE, Karlyshev AV, Chernovskaya TV et al (1991) Expression of the envelope antigen F1 of Yersinia pestis is mediated by the product of caf1M gene having homology with the chaperone PapD of Escherichia coli. FEBS Lett 286:79–82

    Article  PubMed  CAS  Google Scholar 

  • Giske CG, Monnet DL, Cars O et al (2008) Clinical and economic impact of common multidrug-resistant Gram-negative bacilli. Antimicrob Agents Chemother 52:813–821

    Article  PubMed  CAS  Google Scholar 

  • Gupta ML, Sharma A (2007) Pneumonic plague, Northern India, 2002. Emerg Infect Dis 13:664–666

    Article  PubMed  Google Scholar 

  • Huang XZ, Lindler LE (2004) The pH6 antigen is an antiphagocytic factor produced by Yersinia pestis independent of Yersinia outer proteins and capsule antigen. Infect Immun 72:7212–7219

    Article  PubMed  CAS  Google Scholar 

  • Hung DL, Knight SD, Woods RM et al (1996) Molecular basis of two subfamilies of immunoglobulin-like chaperones. EMBO J 15:3792–3805

    PubMed  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

    Article  PubMed  CAS  Google Scholar 

  • Jacob-Dubuisson F, Striker R, Hultgren SJ (1994) Chaperone assisted self-assembly of pili independent of cellular energy. J Biol Chem 269:12447–12455

    PubMed  CAS  Google Scholar 

  • Jedrzejczak R, Dauter Z, Dauter M et al (2006) Structure of DraD invasin from uropathogenic Escherichia coli: a dimer with swapped beta-tails. Acta Crystallogr D Biol Crystallogr 62:157–164

    Article  PubMed  Google Scholar 

  • Karlyshev AV, Galyov EE, Abramov VM et al (1992a) caf1R gene and its role in the regulation of capsule formation of Y. pestis. FEBS Lett 305:37–40

    Article  PubMed  CAS  Google Scholar 

  • Karlyshev AV, Galyov EE, Smirnov OY et al (1992b) A new gene of the f1 operon of Y. pestis involved in the capsule biogenesis. FEBS Lett 297:77–80

    Article  PubMed  CAS  Google Scholar 

  • Karlyshev AV, Galyov EE, Smirnov OY et al (1994) Structure and regulation of a gene cluster involved in capsule formation of Y. pestis. In: Op den Kamp JAF (ed) Biological membranes: structure, biogenesis and dynamic. Springer, New York

    Google Scholar 

  • Knight SD, Berglund J, Choudhury D (2000) Bacterial adhesins: structural studies reveal chaperone function and pilus biogenesis. Curr Opin Chem Biol 4: 653–660

    Article  PubMed  CAS  Google Scholar 

  • Korotkova N, Cota E, Lebedin Y et al (2006a) A subfamily of Dr adhesions of Escherichia coli bind independently to decay-accelerating factor and the N-domain of carcinoembrionic antigen. J Biol Chem 281: 29120–29130

    Article  PubMed  CAS  Google Scholar 

  • Korotkova N, Le Trong I, Samudrala R et al (2006b) Crystal structure and mutational analysis of the DaaE adhesin of Escherichia coli. J Biol Chem 281:22367–22377

    Article  PubMed  CAS  Google Scholar 

  • Korotkova N, Yang Y, Le Trong I et al (2008a) Binding of Dr adhesins of Escherichia coli to carcinoembryonic antigen triggers receptor dissociation. Mol Microbiol 67:420–434

    Article  PubMed  CAS  Google Scholar 

  • Korotkova N, Yarova-Yarovaya Y, Tchesnokova V et al (2008b) Escherichia coli DraE adhesin-associated bacterial internalization by epithelial cells is promoted independently by decay-accelerating factor and carcinoembryonic antigen-related cell adhesion molecule binding and does not require the DraD invasin. Infect Immun 76:3869–3880

    Article  PubMed  CAS  Google Scholar 

  • Kumar S, Balakrishna K, Agarwal GS et al (2009) Th1-type immune response to infection by pYV-cured phoP-phoQ null mutant of Yersinia pseudotuberculosis is defective in mouse model. Antonie Van Leeuwenhoek 95:91–100

    Article  PubMed  CAS  Google Scholar 

  • Lemaitre N, Sebbane F, Long D et al (2006) Yersinia pestis YopJ suppresses tumour necrosis factor alpha induction and contributes to apoptosis of immune cells in the lymph node but is not required for virulence in a rat model of bubonic plague. Infect Immun 74: 5126–5131

    Article  PubMed  CAS  Google Scholar 

  • Li B, Jiang L, Song Q et al (2005) Protein microarray for profiling antibody responses to Yersinia pestis live vaccine. Infect Immun 73:3734–3739

    Article  PubMed  CAS  Google Scholar 

  • Li Y, Cui Y, Hauck Y et al (2009a) Genotyping and phylogenetic analysis of Yersinia pestis by MLVA: insights into the worldwide expansion of Central Asia plague foci. PLoS One 4:e6000

    Article  PubMed  Google Scholar 

  • Li B, Zhou L, Guo J et al (2009b) High-throughput identification of new protective antigens from Yersinia pestis live vaccine by ELISPOT. Infect Immun 77:4356–4361

    Article  PubMed  CAS  Google Scholar 

  • Lindler LE, Tall BD (1993) Yersinia pestis pH6 antigen forms fimbriae and is induced by intracellular association with macrophages. Mol Microbiol 8:311–324

    Article  PubMed  CAS  Google Scholar 

  • Lindler LE, Klempner MS, Straley SC (1990) Yersinia pestis pH6 antigen: genetic, biochemical, and virulence characterization of a protein involved in the pathogenesis of bubonic plague. Infect Immun 58:2569–2577

    PubMed  CAS  Google Scholar 

  • Liu F, Chen H, Galván EM et al (2006) Effects of Psa and F1 on the adhesive and invasive interactions of Yersinia pestis with human respiratory tract epithelial cells. Infect Immun 74:5636–5644

    Article  PubMed  CAS  Google Scholar 

  • Makoveichuk E, Cherepanov P, Lundberg S et al (2003) pH6 antigen of Yersinia pestis interacts with plasma lipoproteins and cell membranes. J Lipid Res 44:320–330

    Article  PubMed  CAS  Google Scholar 

  • Marketon MM, Depaolo RW, Debord KL et al (2005) Plague bacteria target immune cells during infection. Science 309:1739–1741

    Article  PubMed  CAS  Google Scholar 

  • Nishiyama M, Horst R, Eidam OT et al (2005) Structural basis of chaperone–subunit complex recognition by the type 1 pilus assembly platform FimD. EMBO J 24:1–12

    Article  Google Scholar 

  • Payne D, Tatham D, Williamson ED et al (1998) pH6 antigen of Yersinia pestis binds to β1-linked galactosyl residues in glycosphingolipids. Infect Immun 66: 4545–4548

    PubMed  CAS  Google Scholar 

  • Perry RD, Fetherston JD (1997) Yersinia pestis—etiologic agent of plague. Clin Microbiol Rev 10:35–66

    PubMed  CAS  Google Scholar 

  • Pettigrew D, Anderson KL, Billington J et al (2004) High resolution studies of the Afa/Dr adhesin DraE and its interaction with chloramphenicol. J Biol Chem 279:46851–46857

    Article  PubMed  CAS  Google Scholar 

  • Phan G, Remaut H, Wang T et al (2011) Crystal structure of the FimD usher bound to its cognate FimC-FimH substrate. Nature 474:49–53

    Article  PubMed  CAS  Google Scholar 

  • Pujol C, Klein KA, Romanov GA et al (2009) Yersinia pestis can reside in autophagosomes and avoid xenophagy in murine macrophages by preventing vacuole acidification. Infect Immun 77:2251–2261

    Article  PubMed  CAS  Google Scholar 

  • Rasko DA, Webster DR, Sahl JW et al (2011) Origins of the E. coli strain causing an outbreak of hemolytic–uremic syndrome in Germany. N Engl J Med 365(8): 709–717

    Article  PubMed  CAS  Google Scholar 

  • Remaut H, Rose RJ, Hannan TJ et al (2006) Donor-strand exchange in chaperone-assisted pilus assembly proceeds through a concerted β strand displacement mechanism. Mol Cell 22:831–842

    Article  PubMed  CAS  Google Scholar 

  • Remaut H, Tang C, Henderson N et al (2008) Fiber formation across the bacterial outer membrane by the chaperone/usher pathway. Cell 133:640–652

    Article  PubMed  CAS  Google Scholar 

  • Runco LM, Myrczek S, Bliska JB et al (2008) Biogenesis of the fraction 1 capsule and analysis of the ultrastructure of Yersinia pestis. J Bacteriol 190:3381–3385

    Article  PubMed  CAS  Google Scholar 

  • Sauer FG, Futterer K, Pinkner JS et al (1999) Structural basis of chaperone function and pilus biogenesis. Science 285:1058–1061

    Article  PubMed  CAS  Google Scholar 

  • Sauer FG, Barnhart M, Choudhury D et al (2000) Chaperone-assisted pilus assembly and bacterial attachment. Curr Opin Struct Biol 10:548–556

    Article  PubMed  CAS  Google Scholar 

  • Sauer FG, Pinkner JS, Waksman G et al (2002) Chaperone priming of pilus subunits facilitates a topological transition that drives fiber formation. Cell 111:543–551

    Article  PubMed  CAS  Google Scholar 

  • Sauer FG, Remaut H, Hultgren SJ et al (2004) Fiber assembly by the chaperone–usher pathway. Biochim Biophys Acta 1694:259–267

    Article  PubMed  CAS  Google Scholar 

  • Sebbane F, Lemaitre N, Sturdevant DE et al (2006) Adaptive response of Yersinia pestis to extracellular effectors of innate immunity during bubonic plague. Proc Natl Acad Sci U S A 103:11766–11771

    Article  PubMed  CAS  Google Scholar 

  • Sebbane F, Jarrett C, Gardner D et al (2009) The Yersinia pestis caf1M1A1 fimbrial capsule operon promotes transmission by flea bite in a mouse model of bubonic plague. Infect Immun 77:1222–1229

    Article  PubMed  CAS  Google Scholar 

  • Sharma RK, Sodhi A, Batra HV (2005a) Involvement of c-Jun N-terminal kinase in rF1 mediated activation of murine peritoneal macrophages in vitro. J Clin Immunol 3:215–223

    Article  Google Scholar 

  • Sharma RK, Sodhi A, Batra HV et al (2005b) Phosphorylation of p42/44 MAP kinase is required for rF1-induced activation of murine peritoneal macrophages. Mol Immunol 42:1385–1392

    Article  PubMed  CAS  Google Scholar 

  • Smiley ST (2008a) Current challenges in the development of vaccines for pneumonic plague. Expert Rev Vaccines 7:209–221

    Article  PubMed  CAS  Google Scholar 

  • Smiley ST (2008b) Immune defense against pneumonic plague. Immunol Rev 225:256–271

    Article  PubMed  CAS  Google Scholar 

  • Sodhi A, Sharma RK, Batra HV et al (2004) Recombinant fraction 1 protein of Yersinia pestis activates murine peritoneal macrophages in vitro. Cell Immunol 229:52–61

    Article  PubMed  CAS  Google Scholar 

  • Soliakov A, Harris JR, Watkinson A et al (2010) The structure of Yersinia pestis Caf1 polymer in free and adjuvant bound states. Vaccine 28:5746–5754

    Article  PubMed  CAS  Google Scholar 

  • Soto GE, Hultgren SJ (1999) Bacterial adhesins: common themes and variations in architecture and assembly. J Bacteriol 181:1059–1071

    PubMed  CAS  Google Scholar 

  • Thanassi DG, Saulino ET, Hultgren SJ (1998) The chaperone/usher pathway: a major terminal branch of the general secretory pathway. Curr Opin Microbiol 1: 223–231

    Article  PubMed  CAS  Google Scholar 

  • Velan B, Bar-Haim E, Zauberman A et al (2006) Discordance in the effects of Yersinia pestis on dendritic cell functions: induction of maturation and paralysis of migration. Infect Immun 74:6365–6376

    Article  PubMed  CAS  Google Scholar 

  • Verger D, Bullitt E, Hultgren SJ et al (2007) Crystal structure of the P pilus rod subunit PapA. PLoS Pathog 3:e73

    Article  PubMed  Google Scholar 

  • Viboud GI, Bliska JB (2005) Yersinia outer proteins: role in modulation of host cell signaling responses and pathogenesis. Annu Rev Microbiol 59:69–89

    Article  PubMed  CAS  Google Scholar 

  • 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

    Article  PubMed  CAS  Google Scholar 

  • Waksman G, Hultgren SJ (2009) Structural biology of the chaperone–usher pathway of pilus biogenesis. Nat Rev Microbiol 7:765–774

    Article  PubMed  CAS  Google Scholar 

  • Wang H, Cui Y, Wang Z et al (2011) A dog-associated primary pneumonic plague in Qinghai Province, China. Clin Infect Dis 52:185–190

    Article  PubMed  Google Scholar 

  • Welkos SL, Andrews GP, Lindler LE et al (2004) Mu dI1(Ap lac) mutagenesis of Yersinia pestis plasmid pFra and identification of temperature-regulated loci associated with virulence. Plasmid 51:1–11

    Article  PubMed  CAS  Google Scholar 

  • Williamson ED (2009) Plague. Vaccine 27:D56–D60

    Article  PubMed  CAS  Google Scholar 

  • Yang Y, Isberg RR (1997) Transcriptional regulation of the Yersinia pseudotuberculosis pH6 antigen adhesin by two envelope-associated components. Mol Microbiol 24:499–510

    Article  PubMed  CAS  Google Scholar 

  • Zav’yalov VP, Chernovskaya TV, Navolotskaya EV et al (1995a) Specific high affinity binding of human interleukin 1β by Caf1A usher protein of Yersinia pestis. FEBS Lett 371:65–68

    Article  PubMed  Google Scholar 

  • Zav’yalov VP, Zav’yalova GA, Denesyuk AI et al (1995b) Modelling of steric structure of a periplasmic molecular chaperone Caf1M of Yersinia pestis, a prototype member of a subfamily with characteristic structural and functional features. FEMS Immunol Med Microbiol 11:19–24

    Article  PubMed  Google Scholar 

  • Zav’yalov VP, Abramov VM, Cherepanov PG et al (1996) pH6 antigen (PsaA protein) of Yersinia pestis, a novel bacterial Fc-receptor. FEMS Immunol Med Microbiol 14:53–57

    Article  PubMed  Google Scholar 

  • Zav’yalov VP, Chernovskaya TV, Chapman DAG et al (1997) Influence of the conserved disulphide bond exposed to the putative binding pocket, on the structure and function of the immunoglobulin-like periplasmic molecular chaperone, Caf1M, of Yersinia pestis. Biochem J 324:571–578

    PubMed  Google Scholar 

  • Zav’yalov V, Zavialov A, Zav’yalova G et al (2010) Adhesive organelles of Gram negative pathogens assembled with the classical chaperone/usher machinery: structure and function from a clinical standpoint. FEMS Microbiol Rev 34:317–378

    Article  PubMed  Google Scholar 

  • Zavialov AV, Knight SD (2007) A novel self-capping mechanism controls aggregation of periplasmic chaperone Caf1M. Mol Microbiol 64:153–164

    Article  PubMed  CAS  Google Scholar 

  • Zavialov AV, Kersley J, Korpela T et al (2002) Donor strand complementation mechanism in the biogenesis of non-pilus systems. Mol Microbiol 45:983–995

    Article  PubMed  CAS  Google Scholar 

  • Zavialov AV, Berglund J, Pudney AF et al (2003) Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formation. Cell 113:587–596

    Article  PubMed  CAS  Google Scholar 

  • Zavialov AV, Tischenko VM, Fooks LJ et al (2005) Resolving the energy paradox of chaperone-mediated fibre assembly. Biochem J 389:685–694

    Article  PubMed  CAS  Google Scholar 

  • Zavialov A, Zav’yalova G, Korpela T et al (2007) FGL chaperone-assembled fimbrial polyadhesins: anti-immune armament of Gram-negative bacterial pathogens. FEMS Microbiol Rev 31:478–514

    Article  PubMed  CAS  Google Scholar 

  • Zhou H, Monack DM, Kayagaki N et al (2005) Yersinia virulence factor YopJ acts as a deubiquitinase to inhibit NF-kB activation. J Exp Med 202:1327–1332

    Article  PubMed  CAS  Google Scholar 

Download references

Acknowledgements

This work was supported by grants from the European Commission/Research Executive Agency under a Marie Curie International Incoming Fellowship (235538) and a grant from the Academy of Finland (112900).

Author information

Authors and Affiliations

  1. Joint Biotechnology Laboratory, Department of Chemistry, University of Turku, BioCity 6A, Tykistökatu 6, 20520, Turku, Finland

    Vladimir P. Zav’yalov

Authors
  1. Vladimir P. Zav’yalov
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Vladimir P. Zav’yalov .

Editor information

Editors and Affiliations

  1. , Centro de Pesquisa Aggeu Magalhães, Campus da UFPE, Recife, 50670, Brazil

    Alzira Maria Paiva de Almeida

  2. , Centro de Pesquisa Aggeu Magalhães, Campus da UFPE, Recife, 50670-420, Brazil

    Nilma Cintra Leal

Rights and permissions

Reprints and permissions

Copyright information

© 2012 Springer Science+Business Media New York

About this paper

Cite this paper

Zav’yalov, V.P. (2012). Fimbrial Polyadhesins: Anti-immune Armament of Yersinia . In: de Almeida, A., Leal, N. (eds) Advances in Yersinia Research. Advances in Experimental Medicine and Biology, vol 954. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-3561-7_24

Download citation

Publish with us

Policies and ethics

Search

Navigation