Enterococcus faecalis aggregation substance promotes opsonin-independent binding to human neutrophils via a complement receptor type 3-mediated mechanism
Autor: | Natalie N. Vanek, Scott I. Simon, Karen Jacques-Palaz, M.Michele Mariscalco, Gary M. Dunny, Robert M. Rakita |
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Rok vydání: | 1999 |
Předmět: |
Microbiology (medical)
Dose-Response Relationship Drug Neutrophils Immunology Antibodies Monoclonal Macrophage-1 Antigen Membrane Proteins CD47 Antigen General Medicine CHO Cells Opsonin Proteins Microbiology Bacterial Adhesion Infectious Diseases Bacterial Proteins Antigens CD Cricetinae Enterococcus faecalis Immunology and Allergy Animals Humans Receptors Vitronectin Adhesins Bacterial Carrier Proteins Oligopeptides |
Zdroj: | FEMS immunology and medical microbiology. 26(1) |
ISSN: | 0928-8244 |
Popis: | Enterococcus faecalis aggregation substance (AS) mediates efficient adhesion between bacteria, thereby facilitating plasmid exchange as an integral part of a bacterial sex pheromone system. We examined the interaction of AS-bearing E. faecalis with human neutrophils (PMNs), an important component of the host defense system. AS promoted a markedly increased opsonin-independent bacterial binding to PMNs. Adhesion was dependent on the expression of the enterococcal Asc10 protein, which contains two Arg-Gly-Asp (RGD) sequences, and addition of exogenous RGD-containing peptides inhibited AS-mediated binding by 66%. AS-mediated adhesion was inhibited by 85% by anti-human complement receptor type 3 (CR3) monoclonal antibodies or by use of PMNs from a patient with leukocyte adhesion deficiency. However, AS-bearing E. faecalis cells were unable to bind to CHO-Mac-1 cells, expressing functionally active CR3, suggesting the potential need for additional PMN surface receptors for bacterial adhesion. Monoclonal antibodies against integrin-associated protein (CD47) and L-selectin, both of which may interact with CR3 and bind to ligands on E. faecalis, also inhibited AS-dependent binding. The non-opsonic binding of E. faecalis to PMNs may play an important role in this organism's pathogenesis. |
Databáze: | OpenAIRE |
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