The complete nucleotide sequence of region 1 of the CFA/I fimbria! operon of human enterotoxigenic<i>Escherichia coli</i>

Bj, Jordi; Ga, Willshaw; Zeijst, Bernard A.M. van der; Gaastra, Wim

doi:10.3109/10425179209020811

Cited by 38 publications

(27 citation statements)

References 17 publications

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“…Expression of four genes (cfaABCE) in the CFA/I operon is required for assembly of CFA/I fimbriae (17). The same is true for CS1 (cooBACD) and CS2 (cotBACD) (30).…”

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confidence: 71%

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The Major Subunit, CfaB, of Colonization Factor Antigen I from Enterotoxigenic Escherichia coli Is a Glycosphingolipid Binding Protein

Jansson¹,

Tobias

Lebens

et al. 2006

Infect Immun

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Bacterial adherence to mucosal surfaces is an important virulence trait of pathogenic bacteria. Adhesion of enterotoxigenic Escherichia coli (ETEC) to the intestine is mediated by a number of antigenically distinct colonization factors (CFs). One of the most common CFs is CFA/I. This has a fimbrial structure composed of a major repeating subunit, CfaB, and a single tip subunit, CfaE. The potential carbohydrate recognition by CFA/I was investigated by binding CFA/I-fimbriated bacteria and purified CFA/I fimbriae to a large number of variant glycosphingolipids separated on thin-layer chromatograms. For both fimbriated bacteria and purified fimbriae, specific interactions could be identified with a number of nonacid glycosphingolipids. These included glucosylceramide, lactosylceramide with phytosphingosine and/or hydroxy fatty acids, neolactotetraosylceramide, gangliotriaosylceramide, gangliotetraosylceramide, the H5 type 2 pentaglycosylceramide, the Le a -5 glycosphingolipid, the Le x -5 glycosphingolipid, and the Le y -6 glycosphingolipid. These glycosphingolipids were also recognized by recombinant E. coli expressing CFA/I in the absence of tip protein CfaE, as well as by purified fimbriae from the same strain. This demonstrates that the glycosphingolipid-binding capacity of CFA/I resides in the major CfaB subunit.

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“…Expression of four genes (cfaABCE) in the CFA/I operon is required for assembly of CFA/I fimbriae (17). The same is true for CS1 (cooBACD) and CS2 (cotBACD) (30).…”

mentioning

confidence: 71%

“…NeuAc␣8NeuAc␣3Gal␤4Glc␤1Cer Ϫ ND ND 31, GM1 (d18:1-18:0 and d18: [1][2][3][4][5][6][7][8][9][10][11][12][13][14][15][16][17][18][19][20]…”

Section: Resultsunclassified

The Major Subunit, CfaB, of Colonization Factor Antigen I from Enterotoxigenic Escherichia coli Is a Glycosphingolipid Binding Protein

Jansson¹,

Tobias

Lebens

et al. 2006

Infect Immun

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show abstract

“…3). Previous studies (8,102) listed ushers of Burkholderia cepacia (CblC) (282,332), E. coli (CfaC, CooC, CosC, CotC, CsaC, CsbC, CsdC, and CsuC) (7,8,97,99,100,125,164), S. enterica serotype Typhi (TcfC) (72,95), and Yersinia pestis (YPO3798) (254) as being members of the alternate chaperone/usher family. The ␣-fimbrial clade defined in this study includes additional usher proteins, one of which, CsfC (CS5 fimbriae), had not previously been classified as a member of the alternate chaperone/usher family.…”

Section: The Alternate Chaperone/usher Familymentioning

confidence: 99%

Evolution of the Chaperone/Usher Assembly Pathway: Fimbrial Classification Goes Greek

Nuccio

Bäumler

2007

Microbiol Mol Biol Rev

295

456

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SUMMARY Many Proteobacteria use the chaperone/usher pathway to assemble proteinaceous filaments on the bacterial surface. These filaments can curl into fimbrial or nonfimbrial surface structures (e.g., a capsule or spore coat). This article reviews the phylogeny of operons belonging to the chaperone/usher assembly class to explore the utility of establishing a scheme for subdividing them into clades of phylogenetically related gene clusters. Based on usher amino acid sequence comparisons, our analysis shows that the chaperone/usher assembly class is subdivided into six major phylogenetic clades, which we have termed α-, β-, γ-, κ-, π-, and σ-fimbriae. Members of each clade share related operon structures and encode fimbrial subunits with similar protein domains. The proposed classification system offers a simple and convenient method for assigning newly discovered chaperone/usher systems to one of the six major phylogenetic groups.

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“…This family includes coli surface antigen 1 (CS1), CS2, CS4, CS14, CS17, CS19, and putative CF O71 (PCFO71). The complete DNA sequences of the gene clusters encoding CFA/I, CS1, and CS2 have been published previously (11,12,21,36,49). The genes for the major subunit of two of the other related fimbriae have been reported previously (13,15).…”

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confidence: 99%

Evolutionary and Functional Relationships of Colonization Factor Antigen I and Other Class 5 Adhesive Fimbriae of Enterotoxigenic Escherichia coli

et al. 2004

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Colonization factor antigen I (CFA/I) is the archetype of eight genetically related fimbriae of enterotoxigenic Escherichia coli (ETEC) designated class 5 fimbriae. Assembled by the alternate chaperone pathway, these organelles comprise a rigid stalk of polymerized major subunits and an apparently tip-localized minor adhesive subunit. We examined the evolutionary relationships of class 5-specific structural proteins and correlated these with functional properties. We sequenced the gene clusters encoding coli surface antigen 4 (CS4), CS14, CS17, CS19, and putative colonization factor antigen O71 (PCFO71) and analyzed the deduced proteins and the published homologs of CFA/I, CS1, and CS2. Multiple alignment and phylogenetic analysis of the proteins encoded by each operon define three subclasses, 5a (CFA/I, CS4, and CS14), 5b (CS1, CS17, CS19, and PCFO71), and 5c (CS2). These share distant evolutionary relatedness to fimbrial systems of three other genera. Subclass divisions generally correlate with distinguishing in vitro adherence phenotypes of strains bearing the ETEC fimbriae. Phylogenetic comparisons of the individual structural proteins demonstrated greater intrasubclass conservation among the minor subunits than the major subunits. To correlate this with functional attributes, we made antibodies against CFA/I and CS17 whole fimbriae and maltose-binding protein fusions with the amino-terminal half of the corresponding minor subunits. Anti-minor subunit Fab preparations showed hemagglutination inhibition (HAI) of ETEC expressing homologous and intrasubclass heterologous colonization factors while anti-fimbrial Fab fractions showed HAI activity limited to colonization factor-homologous ETEC. These results were corroborated with similar results from the Caco-2 cell adherence assay. Our findings suggest that the minor subunits of class 5 fimbriae may be superior to whole fimbriae in inducing antiadhesive immunity.

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The complete nucleotide sequence of region 1 of the CFA/I fimbria! operon of human enterotoxigenicEscherichia coli

Cited by 38 publications

References 17 publications

The Major Subunit, CfaB, of Colonization Factor Antigen I from Enterotoxigenic Escherichia coli Is a Glycosphingolipid Binding Protein

The Major Subunit, CfaB, of Colonization Factor Antigen I from Enterotoxigenic Escherichia coli Is a Glycosphingolipid Binding Protein

Evolution of the Chaperone/Usher Assembly Pathway: Fimbrial Classification Goes Greek

Evolutionary and Functional Relationships of Colonization Factor Antigen I and Other Class 5 Adhesive Fimbriae of Enterotoxigenic Escherichia coli

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