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Gene Review

fimI  -  fimbrin-like protein FimI

Salmonella enterica subsp. enterica serovar Typhimurium str. LT2

 
 
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Disease relevance of fimI

 

High impact information on fimI

  • Furthermore, attachment to and invasion of bladder epithelial cells, which were mediated much better by native E. coli type 1 fimbriae compared with native K. pneumoniae type 1 fimbriae, were found to be dependent on the background of the fimbrial shaft (E. coli versus K. pneumoniae) rather than the background of the FimH expressed [5].
  • The capacity of type 1 fimbrial shafts to modulate the tissue tropism of different enterobacterial species represents a novel function for these highly organized structures [5].
  • Characterization of the fimH genes, encoding the fimbrial adhesins, indicated two allelic variants [6].
  • Methylation of the pef GATC II site appeared to be required for pef fimbrial expression based on analysis of a GCTC II mutant that did not express Pef fimbriae [7].
  • Nucleotide sequence of a 13.9 kb segment of the 90 kb virulence plasmid of Salmonella typhimurium: the presence of fimbrial biosynthetic genes [4].
 

Chemical compound and disease context of fimI

 

Biological context of fimI

  • The differences in genetic organization and protein sequence relatedness from other fimbrial gene clusters suggest that the pef locus might encode a novel type of fimbria [4].
  • Between the pef and the repB loci, there were five open reading frames, one of which (orf8) gave rise to active PhoA fusions but was not necessary for fimbrial expression [4].
  • In addition, the origin of transcription has been identified and is located 120 base pairs upstream of the fimA initiation codon [3].
  • To address this question, we constructed mutations in all four known fimbrial operons of S. typhimurium: fim, lpf, pef, and agf [10].
  • The novel fimbrial operon was absent from the S. typhi genome [9].
 

Anatomical context of fimI

  • Because these fimbrial types bind to laminin of basement membranes (M. Kukkonen et al., Mol. Microbiol. 7:229-237, 1993; S. Saarela et al., Infect. Immun. 64:2857-2860, 1996), the results demonstrate a structural unity in the creation and targeting of bacterium-bound proteolytic plasmin activity to basement membranes [11].
  • The identification of five fimbrial gene clusters was of particular interest, as we have demonstrated that type 1 fimbriae are required for biofilm formation on HEp-2 cells and murine intestinal epithelium [12].
  • Therefore, FimZ represents a molecular connection between flagella and fimbrial formation in serovar Typhimurium, indicating that the synthesis of flagella and fimbriae are oppositely controlled [13].
  • When fimbriate (Fim+) strains of Salmonella typhimurium were grown in static broth, many bacteria were in the fimbriate phase and bore fimbrial mannose-sensitive haemagglutinin (MSHA) that enabled them to adhere to guinea-pig and other erythrocytes and to agglutinate them in rocked tile and static settling tests [14].
 

Associations of fimI with chemical compounds

  • To better understand the specific role of FimW in fimbrial expression, a mutation was constructed in this gene by the insertion of a kanamycin resistance DNA cassette into the chromosome [15].
  • Three different antigens were tested: S. enteritidis flagella, SEF14 (a 14-kDa fimbrial protein produced ostensibly by S. enteritidis), and a sodium deoxycholate extract of whole S. enteritidis organism [16].
  • Seroreactivity of Salmonella-infected cattle herds against a fimbrial antigen in comparison with lipopolysaccharide antigens [17].
 

Regulatory relationships of fimI

 

Other interactions of fimI

  • The fimZ mutant demonstrated decreased levels of fimA expression compared with the parental strain when both were grown under conditions favoring fimbrial expression [19].
  • Other loci of the plasmid, such as the fimbrial operon pef, the conjugal transfer gene traT and the enigmatic rck and rsk loci, may play a role in other stages of the infection process [20].
  • A single gene, fimA, encodes the major fimbrial unit [21].
  • The pefA gene which encoded the serotype associated plasmid (SAP) mediated fimbrial major subunit antigen of Salmonella enterica serotype Typhimurium shared genetic identity with 128 of 706 salmonella isolates as demonstrated by dot (colony) hybridization [22].
  • The lpf fimbrial operon oscillates between phase ON and phase OFF expression states, thereby generating heterogeneity within S. enterica serotype Typhimurium populations with regard to expression of long polar fimbrial antigens [23].
 

Analytical, diagnostic and therapeutic context of fimI

References

  1. Phase variation of the lpf operon is a mechanism to evade cross-immunity between Salmonella serotypes. Norris, T.L., Bäumler, A.J. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  2. Mast cells process bacterial Ags through a phagocytic route for class I MHC presentation to T cells. Malaviya, R., Twesten, N.J., Ross, E.A., Abraham, S.N., Pfeifer, J.D. J. Immunol. (1996) [Pubmed]
  3. Characterization of the type 1 fimbrial subunit gene (fimA) of Serratia marcescens. Nichols, W.A., Clegg, S., Brown, M.R. Mol. Microbiol. (1990) [Pubmed]
  4. Nucleotide sequence of a 13.9 kb segment of the 90 kb virulence plasmid of Salmonella typhimurium: the presence of fimbrial biosynthetic genes. Friedrich, M.J., Kinsey, N.E., Vila, J., Kadner, R.J. Mol. Microbiol. (1993) [Pubmed]
  5. The distinct binding specificities exhibited by enterobacterial type 1 fimbriae are determined by their fimbrial shafts. Duncan, M.J., Mann, E.L., Cohen, M.S., Ofek, I., Sharon, N., Abraham, S.N. J. Biol. Chem. (2005) [Pubmed]
  6. Differential binding to and biofilm formation on, HEp-2 cells by Salmonella enterica serovar Typhimurium is dependent upon allelic variation in the fimH gene of the fim gene cluster. Boddicker, J.D., Ledeboer, N.A., Jagnow, J., Jones, B.D., Clegg, S. Mol. Microbiol. (2002) [Pubmed]
  7. DNA methylation-dependent regulation of pef expression in Salmonella typhimurium. Nicholson, B., Low, D. Mol. Microbiol. (2000) [Pubmed]
  8. Carbohydrate-binding sites of the mannose-specific fimbrial lectins of enterobacteria. Firon, N., Ofek, I., Sharon, N. Infect. Immun. (1984) [Pubmed]
  9. Genomic subtractive hybridization and selective capture of transcribed sequences identify a novel Salmonella typhimurium fimbrial operon and putative transcriptional regulator that are absent from the Salmonella typhi genome. Morrow, B.J., Graham, J.E., Curtiss, R. Infect. Immun. (1999) [Pubmed]
  10. Multiple fimbrial adhesins are required for full virulence of Salmonella typhimurium in mice. van der Velden, A.W., Bäumler, A.J., Tsolis, R.M., Heffron, F. Infect. Immun. (1998) [Pubmed]
  11. Identification of two laminin-binding fimbriae, the type 1 fimbria of Salmonella enterica serovar typhimurium and the G fimbria of Escherichia coli, as plasminogen receptors. Kukkonen, M., Saarela, S., Lähteenmäki, K., Hynönen, U., Westerlund-Wikström, B., Rhen, M., Korhonen, T.K. Infect. Immun. (1998) [Pubmed]
  12. Salmonella enterica serovar Typhimurium requires the Lpf, Pef, and Tafi fimbriae for biofilm formation on HEp-2 tissue culture cells and chicken intestinal epithelium. Ledeboer, N.A., Frye, J.G., McClelland, M., Jones, B.D. Infect. Immun. (2006) [Pubmed]
  13. FimZ is a molecular link between sticking and swimming in Salmonella enterica serovar Typhimurium. Clegg, S., Hughes, K.T. J. Bacteriol. (2002) [Pubmed]
  14. Haemagglutinins and adhesion of Salmonella typhimurium to HEp2 and HeLa cells. Tavendale, A., Jardine, C.K., Old, D.C., Duguid, J.P. J. Med. Microbiol. (1983) [Pubmed]
  15. FimW is a negative regulator affecting type 1 fimbrial expression in Salmonella enterica serovar typhimurium. Tinker, J.K., Hancox, L.S., Clegg, S. J. Bacteriol. (2001) [Pubmed]
  16. Application of the agar gel precipitin test to detect antibodies to Salmonella enterica serovar enteritidis in serum and egg yolks from infected hens. Holt, P.S., Stone, H.D., Gast, R.K., Greene, C.R. Poult. Sci. (2000) [Pubmed]
  17. Seroreactivity of Salmonella-infected cattle herds against a fimbrial antigen in comparison with lipopolysaccharide antigens. Hoorfar, J., Lind, P., Bell, M.M., Thorns, C.J. Zentralblatt Veterinarmedizin Reihe B (1996) [Pubmed]
  18. PCR amplification of the Salmonella typhimurium fimY gene sequence to detect the Salmonella species. Yeh, K.S., Chen, T.H., Liao, C.W., Chang, C.S., Lo, H.C. Int. J. Food Microbiol. (2002) [Pubmed]
  19. Construction and characterization of a fimZ mutant of Salmonella typhimurium. Yeh, K.S., Hancox, L.S., Clegg, S. J. Bacteriol. (1995) [Pubmed]
  20. The virulence plasmids of Salmonella. Rotger, R., Casadesús, J. Int. Microbiol. (1999) [Pubmed]
  21. PCR amplification of the fimA gene sequence of Salmonella typhimurium, a specific method for detection of Salmonella spp. Cohen, H.J., Mechanda, S.M., Lin, W. Appl. Environ. Microbiol. (1996) [Pubmed]
  22. Distribution, gene sequence and expression in vivo of the plasmid encoded fimbrial antigen of Salmonella serotype Enteritidis. Woodward, M.J., Allen-Vercoe, E., Redstone, J.S. Epidemiol. Infect. (1996) [Pubmed]
  23. Population heterogeneity of Salmonella enterica serotype Typhimurium resulting from phase variation of the lpf operon in vitro and in vivo. Kingsley, R.A., Weening, E.H., Keestra, A.M., Bäumler, A.J. J. Bacteriol. (2002) [Pubmed]
  24. Identification and sequence analysis of lpfABCDE, a putative fimbrial operon of Salmonella typhimurium. Bäumler, A.J., Heffron, F. J. Bacteriol. (1995) [Pubmed]
 
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