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Gene Review

fimX  -  fimbrial protein

Bordetella pertussis Tohama I

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Disease relevance of fimX


High impact information on fimX

  • Its amino acid sequence shares similarities with those of the fimbrial subunits [6].
  • We propose that these mutations affect transcription of the fim genes by varying the distance between the binding site for an activator and the -10 box [2].
  • Nonopsonized Bordetella pertussis bind to human monocytes by means of the virulence factors filamentous hemagglutinin (FHA), pertactin, and the minor fimbrial subunit FimD [7].
  • The primary structure of FimD, derived from the DNA sequence of its gene, showed homology with a number of fimbrial adhesins [8].
  • An insertion mutation in fimB abolished the expression of fimbrial subunits, implicating this gene in the biosynthesis of both serotype 2 and 3 fimbriae [9].

Chemical compound and disease context of fimX


Biological context of fimX


Anatomical context of fimX

  • The ability of the two fimbrial mutants to colonize the nasopharynx, trachea, and lungs was compared with those of the wild type parental strain and a filamentous hemagglutinin (FHA) mutant [13].
  • These subunits are connected by interactions along the fimbrial backbone which, unlike other classes of bacterial fimbriae, has no axial channel [14].
  • The results obtained with the two types of fimbrial subunits were generally the same: a recombinant protein of the expected molecular mass (19.2 kDa) was present in the periplasm of the leaky mutants and of CAG629 strain (Ion protease- and heat shock protease-deficient) [15].

Associations of fimX with chemical compounds

  • The protein deduced from the nucleotide sequence shows good agreement with the NH2-terminal amino acid sequence, amino acid composition and molecular weight of the purified fimbrial subunit [16].
  • The fimbrial agglutinogens recognized by the monoclonal antibodies were also uniquely reactive with either U.S. Reference Factor 2 or 6 antiserum (Eldering agglutinogen 2 or 6 polyclonal antiserum) in an indirect ELISA [17].
  • The major heparin binding regions identified in Fim2 are part of epitopes recognized by human antibodies, suggesting that the heparin binding regions are exposed at the fimbrial surface and are immunodominant [18].
  • By Western blot (immunoblot), it was determined that monoclonal antibody CF8 does not react with proteins denatured by treatment with sodium dodecyl sulfate and beta-mercaptoethanol and by boiling for 5 min but that it does recognize fimbrial proteins in their native, nondenatured state [19].
  • These include genes coding for the synthesis of a polysaccharide capsule, hemagglutinins, a type I secretion system adjacent to two very large genes for secreted proteins, and unique genes for both lipopolysaccharide and fimbrial biogenesis [20].

Other interactions of fimX


Analytical, diagnostic and therapeutic context of fimX


  1. Nucleotide sequence of the fim3 gene from Bordetella pertussis and homology to fim2 and fimX gene products. Cuzzoni, A., Pedroni, P., Riboli, B., Grandi, G., de Ferra, F. Nucleic Acids Res. (1990) [Pubmed]
  2. Fimbrial phase variation in Bordetella pertussis: a novel mechanism for transcriptional regulation. Willems, R., Paul, A., van der Heide, H.G., ter Avest, A.R., Mooi, F.R. EMBO J. (1990) [Pubmed]
  3. Engineering upstream transcriptional and translational signals of Bordetella pertussis serotype 2 fimbrial subunit protein for efficient expression in Escherichia coli: in vitro autoassembly of the expressed product into filamentous structures. Walker, M.J., Rohde, M., Brownlie, R.M., Timmis, K.N. Mol. Microbiol. (1990) [Pubmed]
  4. Construction and analysis of Bordetella pertussis mutants defective in the production of fimbriae. Mooi, F.R., Jansen, W.H., Brunings, H., Gielen, H., van der Heide, H.G., Walvoort, H.C., Guinee, P.A. Microb. Pathog. (1992) [Pubmed]
  5. Characterization of fimbrial subunits from Bordetella species. Mooi, F.R., van der Heide, H.G., ter Avest, A.R., Welinder, K.G., Livey, I., van der Zeijst, B.A., Gaastra, W. Microb. Pathog. (1987) [Pubmed]
  6. Common accessory genes for the Bordetella pertussis filamentous hemagglutinin and fimbriae share sequence similarities with the papC and papD gene families. Locht, C., Geoffroy, M.C., Renauld, G. EMBO J. (1992) [Pubmed]
  7. Binding of FimD on Bordetella pertussis to very late antigen-5 on monocytes activates complement receptor type 3 via protein tyrosine kinases. Hazenbos, W.L., van den Berg, B.M., Geuijen, C.W., Mooi, F.R., van Furth, R. J. Immunol. (1995) [Pubmed]
  8. Isolation of a putative fimbrial adhesin from Bordetella pertussis and the identification of its gene. Willems, R.J., Geuijen, C., van der Heide, H.G., Matheson, M., Robinson, A., Versluis, L.F., Ebberink, R., Theelen, J., Mooi, F.R. Mol. Microbiol. (1993) [Pubmed]
  9. Characterization of a Bordetella pertussis fimbrial gene cluster which is located directly downstream of the filamentous haemagglutinin gene. Willems, R.J., van der Heide, H.G., Mooi, F.R. Mol. Microbiol. (1992) [Pubmed]
  10. Mouse-protecting and histamine-sensitizing activities of pertussigen and fimbrial hemagglutinin from Bordetella pertussis. Munoz, J.J., Arai, H., Cole, R.L. Infect. Immun. (1981) [Pubmed]
  11. Cloning of a novel pilin-like gene from Bordetella pertussis: homology to the fim2 gene. Pedroni, P., Riboli, B., de Ferra, F., Grandi, G., Toma, S., Aricò, B., Rappuoli, R. Mol. Microbiol. (1988) [Pubmed]
  12. Characterization of fimN, a new Bordetella bronchiseptica major fimbrial subunit gene. Kania, S.A., Rajeev, S., Burns, E.H., Odom, T.F., Holloway, S.M., Bemis, D.A. Gene (2000) [Pubmed]
  13. Role of the Bordetella pertussis minor fimbrial subunit, FimD, in colonization of the mouse respiratory tract. Geuijen, C.A., Willems, R.J., Bongaerts, M., Top, J., Gielen, H., Mooi, F.R. Infect. Immun. (1997) [Pubmed]
  14. Three-dimensional structure of Bordetella pertussis fimbriae. Heck, D.V., Trus, B.L., Steven, A.C. J. Struct. Biol. (1996) [Pubmed]
  15. Export of Bordetella pertussis serotype 2 and 3 fimbrial subunits by Escherichia coli. Guzmàn, C.A., Piatti, G., Staendner, L.H., Biavasco, F., Pruzzo, C. FEMS Microbiol. Lett. (1995) [Pubmed]
  16. Cloning and nucleotide sequence analysis of the serotype 2 fimbrial subunit gene of Bordetella pertussis. Livey, I., Duggleby, C.J., Robinson, A. Mol. Microbiol. (1987) [Pubmed]
  17. Comparison of type 2 and type 6 fimbriae of Bordetella pertussis by using agglutinating monoclonal antibodies. Li, Z.M., Brennan, M.J., David, J.L., Carter, P.H., Cowell, J.L., Manclark, C.R. Infect. Immun. (1988) [Pubmed]
  18. Identification and characterization of heparin binding regions of the Fim2 subunit of Bordetella pertussis. Geuijen, C.A., Willems, R.J., Hoogerhout, P., Puijk, W.C., Meloen, R.H., Mooi, F.R. Infect. Immun. (1998) [Pubmed]
  19. Fimbriae and determination of host species specificity of Bordetella bronchiseptica. Burns, E.H., Norman, J.M., Hatcher, M.D., Bemis, D.A. J. Clin. Microbiol. (1993) [Pubmed]
  20. Comparison of the genome sequence of the poultry pathogen Bordetella avium with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals extensive diversity in surface structures associated with host interaction. Sebaihia, M., Preston, A., Maskell, D.J., Kuzmiak, H., Connell, T.D., King, N.D., Orndorff, P.E., Miyamoto, D.M., Thomson, N.R., Harris, D., Goble, A., Lord, A., Murphy, L., Quail, M.A., Rutter, S., Squares, R., Squares, S., Woodward, J., Parkhill, J., Temple, L.M. J. Bacteriol. (2006) [Pubmed]
  21. Temporal trends in circulating Bordetella pertussis strains in Australia. Poynten, M., McIntyre, P.B., Mooi, F.R., Heuvelman, K.J., Gilbert, G.L. Epidemiol. Infect. (2004) [Pubmed]
  22. Prevalence of pertussis antibodies in maternal delivery, cord, and infant serum. Healy, C.M., Munoz, F.M., Rench, M.A., Halasa, N.B., Edwards, K.M., Baker, C.J. J. Infect. Dis. (2004) [Pubmed]
  23. Use of the promoter fusion transposon Tn5 lac to identify mutations in Bordetella pertussis vir-regulated genes. Weiss, A.A., Melton, A.R., Walker, K.E., Andraos-Selim, C., Meidl, J.J. Infect. Immun. (1989) [Pubmed]
  24. Purification and crystallization of fimbrial hemagglutinin from Bordetella pertussis. Arai, H., Munoz, J.J. Infect. Immun. (1979) [Pubmed]
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