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Gene Review:

EF0485 - aggregation substance

Enterococcus faecalis V583

Waters, C.M. et al., Sartingen, S. et al., Süssmuth, S.D. et al., Waters, C.M. et al., Hirt, H. et al., et al.

Wells, Moore, Hoag, Hirt, Dunny, Erlandsen,

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Disease relevance of EF0485

Aggregation substance (AS), a plasmid-encoded surface protein of Enterococcus faecalis, plays important roles in virulence and antibiotic resistance transfer [1].

High impact information on EF0485

Aggregation substance (AS), a surface protein encoded on the pheromone-inducible plasmids of Enterococcus faecalis, has been shown to increase adherence and internalization into a number of different cell types, presumably through integrin binding mediated by the N-terminal RGD motif of AS [2].
Aggregation substance (AS) on the sex pheromone plasmids of E. faecalis has been implicated as a virulence factor in several model systems [3].
Aggregation substance promotes adherence, phagocytosis, and intracellular survival of Enterococcus faecalis within human macrophages and suppresses respiratory burst [4].
Aggregation substance increases adherence and internalization, but not translocation, of Enterococcus faecalis through different intestinal epithelial cells in vitro [5].

Biological context of EF0485

Aggregation substance (AS) is an Enterococcus faecalis surface protein that may contribute to virulence [6].

Analytical, diagnostic and therapeutic context of EF0485

Aggregation substance could be extracted from induced cells but not uninduced cells as demonstrated by crossed immunoelectrophoresis [7].

References

An amino-terminal domain of Enterococcus faecalis aggregation substance is required for aggregation, bacterial internalization by epithelial cells and binding to lipoteichoic acid. Waters, C.M., Hirt, H., McCormick, J.K., Schlievert, P.M., Wells, C.L., Dunny, G.M. Mol. Microbiol. (2004) [Pubmed]
The aggregation domain of aggregation substance, not the RGD motifs, is critical for efficient internalization by HT-29 enterocytes. Waters, C.M., Wells, C.L., Dunny, G.M. Infect. Immun. (2003) [Pubmed]
In vivo induction of virulence and antibiotic resistance transfer in Enterococcus faecalis mediated by the sex pheromone-sensing system of pCF10. Hirt, H., Schlievert, P.M., Dunny, G.M. Infect. Immun. (2002) [Pubmed]
Aggregation substance promotes adherence, phagocytosis, and intracellular survival of Enterococcus faecalis within human macrophages and suppresses respiratory burst. Süssmuth, S.D., Muscholl-Silberhorn, A., Wirth, R., Susa, M., Marre, R., Rozdzinski, E. Infect. Immun. (2000) [Pubmed]
Aggregation substance increases adherence and internalization, but not translocation, of Enterococcus faecalis through different intestinal epithelial cells in vitro. Sartingen, S., Rozdzinski, E., Muscholl-Silberhorn, A., Marre, R. Infect. Immun. (2000) [Pubmed]
Inducible expression of Enterococcus faecalis aggregation substance surface protein facilitates bacterial internalization by cultured enterocytes. Wells, C.L., Moore, E.A., Hoag, J.A., Hirt, H., Dunny, G.M., Erlandsen, S.L. Infect. Immun. (2000) [Pubmed]
Plasmid content of Streptococcus faecalis strain 39-5 and identification of a pheromone (cPD1)-induced surface antigen. Yagi, Y., Kessler, R.E., Shaw, J.H., Lopatin, D.E., An, F., Clewell, D.B. J. Gen. Microbiol. (1983) [Pubmed]

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