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The TibA adhesin/invasin from enterotoxigenic Escherichia coli is self recognizing and induces bacterial aggregation and biofilm formation.

ABSTRACT: Escherichia coli strains are responsible for many cases of gastrointestinal disease and represent a serious health problem worldwide. An essential step in the pathogenesis of such strains involves recognition and attachment to host intestinal surfaces. TibA is a potent bacterial adhesin associated with a number of enterotoxigenic E. coli strains and mediates bacterial attachment to a variety of human cells; additionally, it promotes invasion of such cells. This adhesin is a surface-displayed autotransporter protein and belongs to the exclusive group of bacterial glycoproteins; only the glycosylated form confers binding to and invasion of mammalian cells. Here we characterized TibA and showed that it possesses self-association characteristics and can mediate autoaggregation of E. coli cells. We demonstrated that intercellular TibA-TibA interaction is responsible for bacterial autoaggregation. Also, TibA expression significantly enhances biofilm formation by E. coli on abiotic surfaces.

SUBMITTER: Sherlock O

PROVIDER: S-EPMC1087433 | biostudies-literature | 2005 Apr

REPOSITORIES: biostudies-literature

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The TibA adhesin/invasin from enterotoxigenic Escherichia coli is self recognizing and induces bacterial aggregation and biofilm formation.

Sherlock Orla O Vejborg Rebecca Munk RM Klemm Per P

Infection and immunity 20050401 4

Escherichia coli strains are responsible for many cases of gastrointestinal disease and represent a serious health problem worldwide. An essential step in the pathogenesis of such strains involves recognition and attachment to host intestinal surfaces. TibA is a potent bacterial adhesin associated with a number of enterotoxigenic E. coli strains and mediates bacterial attachment to a variety of human cells; additionally, it promotes invasion of such cells. This adhesin is a surface-displayed aut ...[more]

PMID: 15784535

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Project description:Enterotoxigenic Escherichia coli (ETEC) strains that produce immunologically heterogeneous fimbriae and enterotoxins are the primary cause of neonatal diarrhea and postweaning diarrhea in young pigs. A multivalent vaccine inducing protective immunity against ideally all ETEC fimbriae and enterotoxins could be effective against diarrhea in young pigs. However, developing a vaccine to broadly protect against various ETEC virulence determinants has proven challenging. Recently developed structure- and epitope-based multiepitope fusion antigen (MEFA) technology that presents neutralizing epitopes of various virulence determinants at a backbone immunogen and that mimics epitope native immunogenicity suggests the feasibility of developing multivalent vaccines. With neutralizing epitopes from ETEC fimbria F18 and enterotoxins being identified, it becomes urgent to identify protective epitopes of K88 (F4) fimbriae, which play a major role in pig neonatal and postweaning diarrhea. In this study, we identified B-cell immunodominant epitopes in silico from the K88ac fimbrial major subunit (also adhesin) FaeG and embedded each epitope in a heterogeneous carrier for epitope fusions. We then immunized mice with each epitope fusion protein and examined epitope antigenicity and also neutralizing activities of epitope-induced antibodies. Data showed that while all nine FaeG epitope fusions induced antibodies to K88ac fimbria, anti-K88 IgG antibodies derived from epitopes MTGDFNGSVD (ep1), LNDLTNGGTK (ep2), GRTKEAFATP (ep3), ELRKPDGGTN (ep4), PMKNAGGTKVGAVKVN (ep5), and RENMEYTDGT (ep8) significantly inhibited adherence of K88ac fimbrial bacteria to porcine intestinal cell line IPEC-J2, indicating that these peptides were the neutralizing epitopes of K88ac fimbrial major subunit FaeG and suggesting the future application of FaeG epitopes in ETEC vaccine development.IMPORTANCE Enterotoxigenic Escherichia coli (ETEC) strains producing K88ac fimbriae and enterotoxins are a major cause of porcine neonatal diarrhea and postweaning diarrhea in the United States. Currently, there is no vaccine to induce broadly protective antiadhesin and antitoxin immunity against ETEC-associated diarrhea. To develop a broadly effective ETEC vaccine, we need to target the most important if not all ETEC virulence determinants. While conventional vaccinology approaches encounter difficulties at integrating or including heterogeneous ETEC fimbria and toxin antigens into a vaccine product, multiepitope fusion antigen (MEFA) structural vaccinology provides a new platform to combine neutralizing antigenic elements or epitopes from various heterogeneous virulence factors for broad immunity and protection. Identification of the neutralizing epitopes of K88ac fimbria from this study added the last antigens to an MEFA-based multivalent vaccine against ETEC-associated diarrhea in pigs. An effective vaccine against pig diarrhea can significantly improve swine health and well-being and reduce economic losses to the swine industry worldwide.

Dataset Information

The TibA adhesin/invasin from enterotoxigenic Escherichia coli is self recognizing and induces bacterial aggregation and biofilm formation.

Publications

The TibA adhesin/invasin from enterotoxigenic Escherichia coli is self recognizing and induces bacterial aggregation and biofilm formation.

Similar Datasets

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