Lack of functional complementation between Bordetella pertussis filamentous hemagglutinin and Proteus mirabilis HpmA hemolysin secretion machineries

Journal of Bacteriology

Volumn 179, Issue 3, 1997, Pages 775-783

  Jacob Dubuisson, Françoise ^a   Buisine, Corinne ^a   Willery, Eve ^a   Renauld Mongénie, Geneviève ^a,b   Locht, Camille ^a  

^a INSTITUT PASTEUR DE LILLE   (France)

^b Pasteur Merieux Connaught   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; CALCIUM ION; HEMAGGLUTININ; HEMOLYSIN; OUTER MEMBRANE PROTEIN; SECRETORY PROTEIN; VIRULENCE FACTOR;

ARTICLE; BORDETELLA PERTUSSIS; ESCHERICHIA COLI; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEUS MIRABILIS; SECRETION; SERRATIA MARCESCENS; SITE DIRECTED MUTAGENESIS;

EID: 0031016583     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.179.3.775-783.1997     Document Type: Article

References (35)

1. Antoine, R., and C. Locht. 1992. Isolation and molecular characterization of a novel broad-host range plasmid from Bordetella bronchiseptica with sequence similarities to plasmids from gram-positive organisms. Mol. Microbiol. 6:1785-1799.
2. Burenkamp, S. J., and E. Leininger. 1992. Cloning, expression, and DNA sequence analysis of genes encoding nontypeable Haemophilus influenzae high-molecular-weight surface-exposed proteins related to filamentous hemagglutinin of Bordetella pertussis. Infect. Immun. 60:1302-1313.
3. Barenkamp, S. J., and J. W. St. Geme III. 1994. Genes encoding high-molecular-weight adhesion proteins of nontypcable Haemophilus influenzae are part of gene clusters. Infect. Immun. 62:3320-3328.
4. Braun, V., S. Hobbie, and R. Ondraczek. 1992. Serratia marcescens forms a new type of cytolysin. FEMS Microbiol, Lett. 100:299-306.
5. Braun, V., R. Ondraczek, S. Hobbie, and T. Focareta. 1992. Activation, secretion and mode of action of the Serratia marcescens haemolysin. Zentralbl. Bakteriol. Suppl. 23:478-488.
6. Cornelis, G. 1994. Yersinia pathogenicity factors. Curr. Top. Microbiol. Immunol. 192:243-263.
7. Cosma, C. L., P. N. Danese, J. H. Carlson, T. J. Silhavy, and W. B. Snyder. 1995. Mutational activation of the Cpx signal transduction pathway of Escherichia coli suppresses the toxicity conferred by certain envelope-associated stresses. Mol. Microbiol. 18:491-505.
8. de Groot, A., A. Filloux, and J. Tommassen. 1991. Conservation of xcp genes, involved in the two-step secretion process, in different Pseudomonas species and other gram-negative bacteria. Mol. Gen. Genet. 229:278-284.
9. Delisse-Gathoye, A.-M., C. Locht, F. Jacob, M. Raaschou-Nielsen, I. Heron, J.-L. Ruelle, M. De Wilde, and T. Cabezon. 1990. Cloning, partial sequence, expression, and antigenic analysis of the filamentous hemagglutinin gene of Bordetella pertussis. Infect. Immun. 58:2895-2905.
10. Domenighini, M., D. Relman, C. Capiau, S. Falkow, A. Prugnola, V. Scarlato, and R. Rappuoli. 1990. Genetic characterization of Bordetella pertussis filamentous haemagglutinin: a protein processed from an unusually large precursor. Mol. Microbiol. 4:787-800.
11. Fath, M. J., R. C. Skvirsky, and R. Kolter. 1991. Functional complementation between bacterial MDR-like export systems: colicin V, alpha-hemolysin, and Erwinia protease. J. Bacteriol. 173:7549-7556.
12. Forsberg, A., R. Rosqvist, and H. Wolf-Watz. 1994. Regulation and polarized transfer of the Yersinia outer proteins (Yops) involved in antiphagocytosis. Trends Microbiol. 2:14-19.
13. Fürs te, J. P., W. Pansegrau, R. Frank, H. Blöcker, P. Scholz, M. Bagdasarian, and E. Lanka. 1986, Molecular cloning of the plasmid RP4 primase region in a multi-host-range tacP expression vector. Gene 48:119-131.
14. He, S. Y., M. Lindberg, A. K. Chatterjee, and A. Collmer. 1991. Cloned Erwinia chrysanthemi out genes enable Escherichia coli to selectively secrete a diverse family of heterologous proteins into its milieu. Proc. Natl. Acad. Sci. USA 88:1079-1083.
15. Jacob-Dubuisson, F., C. Buisine, N. Mielcarek, E. Clément, F. D. Menozzi, and C. Locht. 1996. Ammo-terminal maturation of the Bordetella pertussis filamentous haemagglutinin (FHA) upon secretion. Mol. Microbiol. 19:65-78.
16. Kovach, M. E., R. W. Phillips, P. H. Elzer, R. M. I. Roop, and K. M. Peterson. 1994, pBBR1-MCS: a broad-host-range cloning vector. BioTechniques 16:800-802.
17. Létoffé, S., J. M. Ghigo, and C. Wandersman. 1994. Secretion of the Serratia marcescens HasA protein by an ABC transporter. J. Bacteriol. 176:5372-5377.
18. Lindeberg, M., G. P. C. Salmond, and A. Collmer. 1996. Complementation of deletion mutations in a cloned functional cluster of Erwinia chrysanthemi out genes with Erwinia carotovora out homologues reveals OutC and OutD as candidate gatekeepers of species-specific secretion of proteins via the type II pathway. Mol. Mierobiol. 20:175-190.
19. Locht, C., P. Bertin, F. D. Menozzi, and G. Renauld. 1993. The filamentous haemagglutinin, a multifaceted adhesin produced by virulent Bordetella spp. Mol. Microbiol. 9:653-660.
20. Locht, C., M.-C. Geoffroy, and G. Renauld. 1992. Common accessory genes for the Bordetella pertussis filamentous haemagglutinin and fimbriae share sequence similarities with the papC and papD gene families. EMBO J. 11:3175-3183.
21. Menozzi, F. D., R. Mutombo, G. Renauld, C. Gantiez, J. H. Hannah, E. Leininger, M. J. Brennan, and C. Locht. 1994, Heparin-inhibitable lectin activity of the filamentous hemagglutinin adhesin of Bordetella pertussis. Infect. Immun. 62:769-778.
22. Ondraczek, R., S. Hobbie, and V. Braun. 1992. In vitro activation of the Serratia marcescens hemolysin through modification and complementation. J. Bacteriol. 174:5086-5094.
23. Overbye, L. J., M. Sandkvist, and M. Bagdasarian. 1993. Genes required for extracellular secretion of enterotoxin are clustered in Vibrio cholerae. Gene 132:101-106.
24. Palmer, K. L., and R. S. J. Munson. 1995. Cloning and characterization of the genes encoding the haemolysin of Haemophilus ducreyi. Mol. Microbiol. 18:821-830.
25. Poole, K., E. Schiebel, and V. Braun. 1988. Molecular characterization of the hemolysin determinant of Serratia marcesens. J. Bacteriol. 170:3177-3188.
26. Pugsley, A. P. 1993. The complete general secretory pathway in gram-negative bacteria. Microbiol. Rev. 57:50-108.
27. Relman, D. A., M. Domenighini, E. Tunomanen, R. Rappuoli, and S. Falkow. 1989. Filamentous hemagglutinin of Bordetella pertussis: nucleotide sequence and crucial role in adherence. Proc. Natl. Acad. Sci. USA 86:2637-2641.
28. Renauld-Mongénie, G., J. Cornette, N. Mielcarek, F. D. Menozzi, and C. Locht. 1996. Distinct roles of the N-terminal and the C-terminal precursor domains in the biogenesis of the Bordetella pertussis filamentous hemagglutinin. J. Bacteriol. 178:1053-1060.
29. Rosqvist, R., S. Hakaasson, A. Forsberg, and H. Wolf-Watz. 1995. Func- tional conservation of the secretion and translocation machinery for virulence proteins of yersiniae, salmonellae and shigellae. EMBO J. 14:4187-4195.
30. Schiebel, E., H. Schwarz, and V. Braun. 1989. Subcellular localization and unique secretion of the hemolysin of Serratia marcescens. J. Biol. Chem. 264:16311-16320.
31. Schönherr, R., R. Tsolis, T. Focareta, and V. Braun. 1993. Ammo acid replacements in the Serratia marcescens haemolysin ShlA define sites involved in activation and secretion. Mol. Microbiol. 9:1229-1237.
32. Totten, P. A., D. V. Norn, and W. E. Stamm. 1995. Characterization of the hemolytte activity of Haemophilus ducreyi. Infect. Immun. 63:4409-4416.
33. Uphoff, T. S., and R. A. Welch. 1990. Nucleotide sequencing of the Proteus mirabilis calcium-independent hemolysin genes (hpmA and hpmB) reveals sequence similarity with the Serratia marcescens hemolysin genes (shlA and shlB). J. Bacteriol. 172:1206-1216.
34. Welch, R. A. 1987. Identification of two different hemolysin determinants in uropathogenic Proteus isolates. Infect. Immun. 55:2183-2190.
35. Willems R. J. C., C. Geuijen, H. G. J. van der Heide, G. Renauld, P. Bertin, W. M. R. van den Akker, C. Locht, and F. R. Mooi. 1994. Mutational analysis of the Bordetella pertussis fim/fha gene cluster: identification of a gene with sequence similarities to haemolysin accessory genes involved in export of FHA. Mol. Microbiol. 11:337-347.