Identification of minor fimbrial subunits involved in biosynthesis of K88 fimbriae

Bakker, Douwe; Willemsen, P.T.J.; Willems, Roland; Huisman, Tako T.; Mooi, Frits R.; Oudega, Bauke; Stegehuis, Freek; Graaf, Frits K. de

doi:10.1128/jb.174.20.6350-6358.1992

Cited by 42 publications

(46 citation statements)

References 26 publications

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“…Minor fimbrial subunits have been implicated in the adherence of F18 fimbriae and AF/R1 fimbriae (48,148,307). However, in the case of F4 and F5 fimbriae, minor subunits are dispensable for adherence (22,303,304), and the major fimbrial subunits (FaeG and FanC) have been implicated in determining the binding activity of their respective adhesins (21,156,250).…”

Section: The -Fimbriae: Flexible Fibrillaementioning

confidence: 99%

“…7). The -fimbriae (FUP cluster 6) (367) comprise usher proteins required for the assembly of the F4 fimbrial antigen (K88 fimbriae) (FaeD) (20,22,224,245,315,316,338), the F5 fimbrial antigen (K99 fimbriae) (FanD) (1, 20, 149, 151, 247, [275][276][277]303), and the F18 fimbrial antigen (F107 fimbriae) (FedB) (147,148,307) found in porcine and bovine isolates of enterotoxigenic E. coli (51,362). Furthermore, this group includes adherence factor/rabbit 1 (AF/R1) fimbriae (AfrB) (48), an uncharacterized operon of E. coli (CshB), the locus for diffuse adherence (LdaD) of atypical enteropathogenic E. coli (294), plasmid-encoded fimbriae (PefC) of S. enterica serotype Typhimurium (96,218), and an intestinal colonization factor of rabbit enteropathogenic E. coli (RalD) (2).…”

Section: The -Fimbriae: Flexible Fibrillaementioning

confidence: 99%

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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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Section: The -Fimbriae: Flexible Fibrillaementioning

confidence: 99%

Section: The -Fimbriae: Flexible Fibrillaementioning

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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“…Seis genes estruturais estão envolvidos na biogênese da fimbria K88 (Mooi & Graaf 1985). O FaeC é um polipeptídeo com aproximadamente 16,9 KDa e localiza-se na extremidade das fímbrias K88, e portanto, possivelmente tenha uma participação importante na adesão da fímbria ao epitélio intestinal (Bakker et al 1992).…”

Section: Introdução Introdução Introdução Introdução Introduçãounclassified

Desenvolvimento e avaliação de novas estratégias de imunização contra colibacilose suína

Simionatto¹,

Vaz

Michelon³

et al. 2005

Pesq. Vet. Bras.

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Swine colibacillosis caused by enterotoxigenic Escherichia coli remains one of the main sanitary problems in pig farms. The recombinant DNA technology offers the possibility of developing new immunization strategies. This paper describes the development of a subunit vaccine through the expression and purification of the E. coli K88 FaeC fimbrial protein. The gene that codes for this antigen was amplified by PCR and cloned into an E. coli expression vector fused to a 6X histidine tag. The recombinant protein was purified by affinity chromatography and used for mice immunization. In parallel, the same gene was cloned into an eucariotic expression vector with the addition of the Kozak sequence for improving translation of this gene in muscle cells. The resulting plasmid named pUP310 was purified in large scale and used to immunize mice. The immune response afforded by both forms of immunization was monitored by ELISA. There was an immune response in mice inoculated with pUP310 and purified FaeC. It was possible to detect anti-FaeC antibodies 42 days after the first inoculation. The antibody titer increased with time, being still detectable 7 months after the first inoculation. It is concluded that recombinant FaeC and pUP310 are potential tools for immunization of swine against E. coli K88.INDEX TERMS: Swine colibacillosis, , , , , FaeC, Escherichia coli, DNA vaccine, recombinant vaccine.

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“…coli K88 fimbrial gene faeH (6), suggesting that this region might include genes involved in a novel adherence factor (Fig. 2).…”

Section: Identification and Cloning Of A Locus For Diffuse Adherencementioning

confidence: 99%

Identification and Characterization of the Locus for Diffuse Adherence, Which Encodes a Novel Afimbrial Adhesin Found in Atypical EnteropathogenicEscherichia coli

et al. 2005

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The O26 serogroup of enteropathogenic Escherichia coli (EPEC) is one of the serogroups most frequently implicated in infant diarrhea and is also common among enterohemorrhagic E. coli (EHEC) strains. The most common O26 strains belong to EPEC/EHEC serotype O26:H11 and are generally Shiga toxin (Stx) positive. Stx-negative E. coli strains that are negative for the EPEC EAF plasmid and bundle-forming pilus (Bfp) are classified as atypical EPEC. Here, we report a novel adhesin present in an stx-negative bfpA-negative atypical EPEC O26:H11 strain isolated from an infant with diarrhea. A cloned 15-kb genomic region from this strain, designated the locus for diffuse adherence (lda), confers diffuse adherence on HEp-2 cells when expressed in E. coli K-12. Sequence analysis of lda revealed a G؉C content of 46.8% and 15 open reading frames sharing homology with the E. coli K88 fae and CS31A clp fimbrial operons. The lda region is part of a putative 26-kb genomic island inserted into the proP gene of the E. coli chromosome. Hybridization studies have demonstrated the prevalence of the minor structural subunit gene, ldaH, across E. coli serogroups O5, O26, O111, and O145. A second plasmid-encoded factor that contributed to the Hep-2 adherence of this strain was also identified but was not characterized. Null mutations that abolish adherence to HEp-2 cells can be restored by plasmid complementation. Antiserum raised against the major structural subunit, LdaG, recognizes a 25-kDa protein from crude heat-extracted protein preparations and inhibits the adherence of the E. coli DH5␣ lda ؉ clone to HEp-2 cells. Electron microscopy revealed a nonfimbrial structure surrounding the bacterial cell.

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Identification of minor fimbrial subunits involved in biosynthesis of K88 fimbriae

Cited by 42 publications

References 26 publications

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

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

Desenvolvimento e avaliação de novas estratégias de imunização contra colibacilose suína

Identification and Characterization of the Locus for Diffuse Adherence, Which Encodes a Novel Afimbrial Adhesin Found in Atypical EnteropathogenicEscherichia coli

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