Exfoliatin-producing strains define a fourth agr specificity group in Staphylococcus aureus

Jarraud, S., Lyon, G. J., Figueiredo, A. M., Lina, G., Gerard, L., Vandenesch, F., Etienne, J., Muir, T. W., Novick, R. P. (2000) Exfoliatin-producing strains define a fourth agr specificity group in Staphylococcus aureus. Journal of Bacteriology, 182 (22). pp. 6517-6522. ISSN 0021-9193

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URL: http://www.ncbi.nlm.nih.gov/pubmed/11053400
DOI: 10.1128/​JB.182.22.6517-6522.2000

Abstract

The staphylococcal virulon is activated by the density-sensing agr system, which is autoinduced by a short peptide (autoinducing peptide [AIP]) processed from a propeptide encoded by agrD. A central segment of the agr locus, consisting of the C-terminal two-thirds of AgrB (the putative processing enzyme), AgrD, and the N-terminal half of AgrC (the receptor), shows striking interstrain variation. This finding has led to the division of Staphylococcus aureus isolates into three different agr specificity groups and to the division of non-aureus staphylococci into a number of others. The AIPs cross-inhibit the agr responses between groups. We have previously shown that most menstrual toxic shock strains belong to agr specificity group III but that no strong clinical identity has been associated with strains of the other two groups. In the present report, we demonstrate a fourth agr specificity group among S. aureus strains and show that most exfoliatin-producing strains belong to this group. A striking common feature of group IV strains is activation of the agr response early in exponential phase, at least 2 h earlier than in strains of the other groups. This finding raises the question of the biological significance of the agr autoinduction threshold.

Item Type: Paper
Uncontrolled Keywords: Amino Acid Sequence Bacterial Proteins Exfoliatins Genes, Bacterial Molecular Sequence Data Signal Transduction Staphylococcus aureus Trans-Activators Transcription Factors
CSHL Authors:
Communities: CSHL labs > Lyon lab
Depositing User: Matt Covey
Date Deposited: 10 Dec 2012 20:05
Last Modified: 10 Dec 2012 21:32
PMCID: PMC94802
URI: http://repository.cshl.edu/id/eprint/26278

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