Enterococcus faecalis aggregation substance promotes opsonin-independent binding to human neutrophils via a complement receptor type 3-mediated mechanism

Natalie N. Vanek, Scott I. Simon, Karen Jacques-Palaz, M. Michele Mariscalco, Gary M. Dunny, Robert M. Rakita

Research output: Contribution to journalArticle

56 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)49-60
Number of pages12
JournalFEMS Immunology and Medical Microbiology
Volume26
Issue number1
DOIs
StatePublished - Oct 1999
Externally publishedYes

Fingerprint

Macrophage-1 Antigen
Opsonin Proteins
Neutrophils
Enterococcus faecalis
Monoclonal Antibodies
Bacterial Adhesion
Sex Attractants
L-Selectin
Integrins
Proteins
Leukocytes
Plasmids
Ligands
Bacteria
Enterococcus faecalis aggregation substance

Keywords

  • Aggregation substance
  • Complement receptor
  • Enterococcus faecalis
  • Neutrophil

ASJC Scopus subject areas

  • Immunology
  • Microbiology
  • Infectious Diseases

Cite this

Enterococcus faecalis aggregation substance promotes opsonin-independent binding to human neutrophils via a complement receptor type 3-mediated mechanism. / Vanek, Natalie N.; Simon, Scott I.; Jacques-Palaz, Karen; Mariscalco, M. Michele; Dunny, Gary M.; Rakita, Robert M.

In: FEMS Immunology and Medical Microbiology, Vol. 26, No. 1, 10.1999, p. 49-60.

Research output: Contribution to journalArticle

Vanek, Natalie N. ; Simon, Scott I. ; Jacques-Palaz, Karen ; Mariscalco, M. Michele ; Dunny, Gary M. ; Rakita, Robert M. / Enterococcus faecalis aggregation substance promotes opsonin-independent binding to human neutrophils via a complement receptor type 3-mediated mechanism. In: FEMS Immunology and Medical Microbiology. 1999 ; Vol. 26, No. 1. pp. 49-60.
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