Analysis of functional domains of the Enterococcus faecalis pheromone-induced surface protein aggregation substance

C. M. Waters, Gary M Dunny

Research output: Contribution to journalArticle

42 Citations (Scopus)

Abstract

Pheromone-inducible aggregation substance (AS) proteins of Enterococcus faecalis are essential for high-efficiency conjugation of the sex pheromone plasmids and also serve as virulence factors during host infection. A number of different functions have been attributed to AS in addition to bacterial cell aggregation, including adhesion to host cells, adhesion to fibrin, increased cell surface hydrophobicity, resistance to killing by polymorphonuclear leukocytes and macrophages, and increased vegetation size in an experimental endocarditis model. Relatively little information is available regarding the structure-activity relationship of AS. To identify functional domains, a library of 23 nonpolar 31-amino-acid insertions was constructed in Asc10, the AS encoded by the plasmid pCF10, using the transposons TnlacZ/in and TnphoA/in. Analysis of these insertions revealed a domain necessary for donor-recipient aggregation that extends further into the amino terminus of the protein than previously reported. In addition, insertions in the C terminus of the protein also reduced aggregation. As expected, the ability to aggregate correlates with efficient plasmid transfer. The results also indicated that an increase in cell surface hydrophobicity resulting from AS expression is not sufficient to mediate bacterial aggregation.

Original languageEnglish (US)
Pages (from-to)5659-5667
Number of pages9
JournalJournal of bacteriology
Volume183
Issue number19
DOIs
StatePublished - Oct 8 2001

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Enterococcus faecalis
Pheromones
Membrane Proteins
Plasmids
Hydrophobic and Hydrophilic Interactions
Sex Attractants
Cell Aggregation
Virulence Factors
Structure-Activity Relationship
Protein C
Endocarditis
Fibrin
Cell Adhesion
Libraries
Proteins
Neutrophils
Theoretical Models
Macrophages
Amino Acids
Infection

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Analysis of functional domains of the Enterococcus faecalis pheromone-induced surface protein aggregation substance. / Waters, C. M.; Dunny, Gary M.

In: Journal of bacteriology, Vol. 183, No. 19, 08.10.2001, p. 5659-5667.

Research output: Contribution to journalArticle

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