Structural insights into ail-mediated adhesion in Yersinia pestis

Structure

Volumn 19, Issue 11, 2011, Pages 1672-1682

  Yamashita, Satoshi ^a   Lukacik, Petra ^a   Barnard, Travis J ^a   Noinaj, Nicholas ^a   Felek, Suleyman ^b   Tsang, Tiffany M ^c   Krukonis, Eric S ^b,c   Hinnebusch, B Joseph ^d   Buchanan, Susan K ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b UNIVERSITY OF MICHIGAN SCHOOL OF DENTISTRY   (United States)

^c UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^d NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; FIBRONECTIN; HEPARIN; LAMININ; OUTER MEMBRANE PROTEIN; PROTEIN AIL; PROTEIN OMPX; PROTEIN YOPS; SUCRALFATE; UNCLASSIFIED DRUG;

ARTICLE; BACTERIUM ADHERENCE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; HEP 2 CELL; HOST CELL; HOST PATHOGEN INTERACTION; HYDROPHOBICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT; YERSINIA PESTIS;

AMINO ACID SEQUENCE; BACTERIAL ADHESION; BACTERIAL OUTER MEMBRANE PROTEINS; BACTERIAL PROTEINS; CELL LINE; CRYSTALLOGRAPHY, X-RAY; EXTRACELLULAR MATRIX; EXTRACELLULAR MATRIX PROTEINS; HOST-PATHOGEN INTERACTIONS; HUMANS; LAMININ; MEMBRANE PROTEINS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; SUCROSE; SURFACE PROPERTIES; VIRULENCE FACTORS; YERSINIA PESTIS;

BACTERIA (MICROORGANISMS); RODENTIA; YERSINIA; YERSINIA PESTIS;

EID: 80855144811     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2011.08.010     Document Type: Article

References (31)

1. N.A. Baker, D. Sept, S. Joseph, M.J. Holst, and J.A. McCammon Electrostatics of nanosystems: application to microtubules and the ribosome Proc. Natl. Acad. Sci. USA 98 2001 10037 10041 (Pubitemid 32802969)
2. S.S. Bartra, K.L. Styer, D.M. O'Bryant, M.L. Nilles, B.J. Hinnebusch, A. Aballay, and G.V. Plano Resistance of Yersinia pestis to complement-dependent killing is mediated by the Ail outer membrane protein Infect. Immun. 76 2008 612 622 (Pubitemid 351251731)
3. K. Beck, I. Hunter, and J. Engel Structure and function of laminin: anatomy of a multidomain glycoprotein FASEB J. 4 1990 148 160
4. H.G. Boman, and D.A. Monner Characterization of lipopolysaccharides from Escherichia coli K-12 mutants J. Bacteriol. 121 1975 455 464
5. A.M. Crago, and V. Koronakis Binding of extracellular matrix laminin to Escherichia coli expressing the Salmonella outer membrane proteins Rck and PagC FEMS Microbiol. Lett. 176 1999 495 501 (Pubitemid 29308978)
6. S. Felek, and E.S. Krukonis The Yersinia pestis Ail protein mediates binding and Yop delivery to host cells required for plague virulence Infect. Immun. 77 2009 825 836
7. S. Felek, T.M. Tsang, and E.S. Krukonis Three Yersinia pestis adhesins facilitate Yop delivery to eukaryotic cells and contribute to plague virulence Infect. Immun. 78 2010 4134 4150
8. M. Galimand, E. Carniel, and P. Courvalin Resistance of Yersinia pestis to antimicrobial agents Antimicrob. Agents Chemother. 50 2006 3233 3236 (Pubitemid 44527492)
9. E.J. Heffernan, S. Reed, J. Hackett, J. Fierer, C. Roudier, and D. Guiney Mechanism of resistance to complement-mediated killing of bacteria encoded by the Salmonella typhimurium virulence plasmid gene rck J. Clin. Invest. 90 1992 953 964
10. L. Holm, and J. Park DaliLite workbench for protein structure comparison Bioinformatics 16 2000 566 567
11. V. Kirjavainen, H. Jarva, M. Biedzka-Sarek, A.M. Blom, M. Skurnik, and S. Meri Yersinia enterocolitica serum resistance proteins YadA and ail bind the complement regulator C4b-binding protein PLoS Pathog. 4 2008 e1000140
12. A.M. Kolodziejek, D.R. Schnider, H.N. Rohde, A.J. Wojtowicz, G.A. Bohach, S.A. Minnich, and C.J. Hovde Outer membrane protein X (Ail) contributes to Yersinia pestis virulence in pneumonic plague and its activity is dependent on the lipopolysaccharide core length Infect. Immun. 78 2010 5233 5243
13. A.M. Kolodziejek, D.J. Sinclair, K.S. Seo, D.R. Schnider, C.F. Deobald, H.N. Rohde, A.K. Viall, S.S. Minnich, C.J. Hovde, S.A. Minnich, and G.A. Bohach Phenotypic characterization of OmpX, an Ail homologue of Yersinia pestis KIM Microbiology 153 2007 2941 2951 (Pubitemid 47517055)
14. K. Lähteenmäki, R. Virkola, A. Sarén, L. Emödy, and T.K. Korhonen Expression of plasminogen activator pla of Yersinia pestis enhances bacterial attachment to the mammalian extracellular matrix Infect. Immun. 66 1998 5755 5762 (Pubitemid 28531831)
15. J. Mecsas, R. Welch, J.W. Erickson, and C.A. Gross Identification and characterization of an outer membrane protein, OmpX, in Escherichia coli that is homologous to a family of outer membrane proteins including Ail of Yersinia enterocolitica J. Bacteriol. 177 1995 799 804
16. V.L. Miller, and S. Falkow Evidence for two genetic loci in Yersinia enterocolitica that can promote invasion of epithelial cells Infect. Immun. 56 1988 1242 1248
17. V.L. Miller, K.B. Beer, G. Heusipp, B.M. Young, and M.R. Wachtel Identification of regions of Ail required for the invasion and serum resistance phenotypes Mol. Microbiol. 41 2001 1053 1062 (Pubitemid 36124702)
18. U. Ott, E. Odermatt, J. Engel, H. Furthmayr, and R. Timpl Protease resistance and conformation of laminin Eur. J. Biochem. 123 1982 63 72
19. J. Parkhill, B.W. Wren, N.R. Thomson, R.W. Titball, M.T. Holden, M.B. Prentice, M. Sebaihia, K.D. James, C. Churcher, and K.L. Mungall Genome sequence of Yersinia pestis, the causative agent of plague Nature 413 2001 523 527 (Pubitemid 32938750)
20. J. Pettersson, R. Nordfelth, E. Dubinina, T. Bergman, M. Gustafsson, K.E. Magnusson, and H. Wolf-Watz Modulation of virulence factor expression by pathogen target cell contact Science 273 1996 1231 1233 (Pubitemid 26293214)
21. R. Pieper, S.T. Huang, J.M. Robinson, D.J. Clark, H. Alami, P.P. Parmar, R.D. Perry, R.D. Fleischmann, and S.N. Peterson Temperature and growth phase influence the outer-membrane proteome and the expression of a type VI secretion system in Yersinia pestis Microbiology 155 2009 498 512
22. P. Prehm, G. Schmidt, and S. Stirm On the mutations responsible for the rough phenotype of Escherichia coli B J. Gen. Microbiol. 97 1976 121 124
23. J.L. Prior, P.G. Hitchen, D.E. Williamson, A.J. Reason, H.R. Morris, A. Dell, B.W. Wren, and R.W. Titball Characterization of the lipopolysaccharide of Yersinia pestis Microb. Pathog. 30 2001 49 57 (Pubitemid 32552999)
24. W.S. Pulkkinen, and S.I. Miller A Salmonella typhimurium virulence protein is similar to a Yersinia enterocolitica invasion protein and a bacteriophage lambda outer membrane protein J. Bacteriol. 173 1991 86 93
25. K.S. Rostand, and J.D. Esko Microbial adherence to and invasion through proteoglycans Infect. Immun. 65 1997 1 8 (Pubitemid 27008896)
26. F. Sebbane, N. Lemaître, D.E. Sturdevant, R. Rebeil, K. Virtaneva, S.F. Porcella, and B.J. Hinnebusch Adaptive response of Yersinia pestis to extracellular effectors of innate immunity during bubonic plague Proc. Natl. Acad. Sci. USA 103 2006 11766 11771 (Pubitemid 44182525)
27. R. Thomas, and T. Brooks Attachment of Yersinia pestis to human respiratory cell lines is inhibited by certain oligosaccharides J. Med. Microbiol. 55 2006 309 315
28. T.M. Tsang, S. Felek, and E.S. Krukonis Ail binding to fibronectin facilitates Yersinia pestis binding to host cells and Yop delivery Infect. Immun. 78 2010 3358 3368
29. L. Vandeputte-Rutten, M.P. Bos, J. Tommassen, and P. Gros Crystal structure of Neisserial surface protein A (NspA), a conserved outer membrane protein with vaccine potential J. Biol. Chem. 278 2003 24825 24830 (Pubitemid 37548640)
30. J. Vogt, and G.E. Schulz The structure of the outer membrane protein OmpX from Escherichia coli reveals possible mechanisms of virulence Structure 7 1999 1301 1309 (Pubitemid 29482991)
31. P. Zhang, M. Skurnik, S.S. Zhang, O. Schwartz, R. Kalyanasundaram, S. Bulgheresi, J.J. He, J.D. Klena, B.J. Hinnebusch, and T. Chen Human dendritic cell-specific intercellular adhesion molecule-grabbing nonintegrin (CD209) is a receptor for Yersinia pestis that promotes phagocytosis by dendritic cells Infect. Immun. 76 2008 2070 2079 (Pubitemid 351656140)