Identification and characterization of the locus for diffuse adherence, which encodes a novel afimbrial adhesin found in atypical enteropathogenic Escherichia coli

Identification and characterization of the locus for diffuse adherence, which encodes a novel afimbrial adhesin found in atypical enteropathogenic Escherichia coli

Autor Scaletsky, Isabel CA Autor UNIFESP Google Scholar
Michalski, Jane Google Scholar
Torres, Alfredo G. Google Scholar
Dulguer, Michelle V. Google Scholar
Kaper, James B. Google Scholar
Instituição Univ Maryland
Universidade Federal de São Paulo (UNIFESP)
Univ Texas
Resumo 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, NOT, 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 alpha lda(+) clone to HEp-2 cells. Electron microscopy revealed a nonfimbrial structure surrounding the bacterial cell.
Idioma Inglês
Data de publicação 2005-08-01
Publicado em Infection and Immunity. Washington: Amer Soc Microbiology, v. 73, n. 8, p. 4753-4765, 2005.
ISSN 0019-9567 (Sherpa/Romeo, fator de impacto)
Publicador Amer Soc Microbiology
Extensão 4753-4765
Fonte http://dx.doi.org/10.1128/IAI.73.8.4753-4765.2005
Direito de acesso Acesso aberto Open Access
Tipo Artigo
Web of Science WOS:000230760600033
Endereço permanente http://repositorio.unifesp.br/handle/11600/28394

Exibir registro completo




Arquivo

Nome: WOS000230760600033.pdf
Tamanho: 661.6KB
Formato: PDF
Descrição:
Abrir arquivo

Este item está nas seguintes coleções

Buscar


Navegar

Minha conta