| Aggregation substance of Enterococcus faecalis mediates adhesion to cultured renal tubular cells. | |
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MedLine Citation:
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PMID: 1729187 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The sex pheromone system of Enterococcus faecalis is a unique, highly efficient plasmid collection mechanism for this species. A crucial role in this system is played by an adhesin called aggregation substance which enables the cell-cell contact between donor and recipient strains. The existence of the amino acid motif Arg-Gly-Asp-Ser in the adhesin prompted us to look for a possible binding of E. faecalis cells expressing aggregation substance to eucaryotic cells. We were able to show that the adhesin mediated binding to cultured renal tubular cells (porcine cell line LLC-PK1) via light microscopic, electron microscopic, and enzyme-linked immunosorbent assay-based studies. Synthesis of the adhesin was induced by some component(s) of serum. These data are interpreted to mean that aggregation substance is an adhesin mediating not only cell-cell contact between different E. faecalis strains but also binding of E. faecalis to eucaryotic cells, and therefore it might contribute to virulence. |
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Authors:
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B Kreft; R Marre; U Schramm; R Wirth |
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Publication Detail:
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Type: In Vitro; Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Infection and immunity Volume: 60 ISSN: 0019-9567 ISO Abbreviation: Infect. Immun. Publication Date: 1992 Jan |
Date Detail:
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Created Date: 1992-02-12 Completed Date: 1992-02-12 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 0246127 Medline TA: Infect Immun Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 25-30 Citation Subset: IM |
Affiliation:
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Klinik für Innere Medizin, Medizinische Universität zu Lübeck, Germany. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Amino Acid Sequence Animals Bacterial Adhesion / physiology* Blotting, Western Cell Adhesion Molecules* Cell Communication / physiology Cells, Cultured Enterococcus faecalis / pathogenicity* Enzyme-Linked Immunosorbent Assay Gene Expression Regulation, Bacterial Kidney Tubules / microbiology* Microscopy, Electron Molecular Sequence Data Oligopeptides / physiology Proteins / physiology* Swine |
| Chemical | |
Reg. No./Substance:
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0/Cell Adhesion Molecules; 0/Oligopeptides; 0/Proteins; 0/cell aggregation factors; 94495-17-7/cAD1 bacterial sex hormone |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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