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Peptide methionine sulfoxide reductase (MsrA) is not a major virulence determinant for the oral pathogen Actinobacillus actinomycetemcomitans^a

Department of Microbiology and Molecular Genetics, University of Vermont, Burlington, VT 05405, USA¹
Laboratory of Biochemistry, NHLBI, National Institutes of Health, Bethesda, MD, USA²

Author for correspondence: Keith P. Mintz. Tel: +1 802 656 4271. Fax: +1 802 656 8749. e-mail: kmintz{at}zoo.uvm.edu

Actinobacillus actinomycetemcomitans is an oral pathogen that is a causative agent for periodontal disease as well as other non-oral infections. The chronic inflammation associated with periodontal diseases suggests that the bacterium must be able to neutralize oxygen intermediates to survive in the host tissues. Methionine sulfoxide reductase (MsrA) is an enzyme that has been demonstrated to have a role in protection against oxidative damage and has also been identified to be required for the proper expression or maintenance of functional adhesins on the surface of several pathogenic bacteria. The A. actinomycetemcomitans homologue of msrA has been isolated and a chromosomal insertion mutant constructed by allele replacement mutagenesis. Inactivation of the gene led to a complete loss of enzymic activity toward a synthetic substrate. However, the isogenic mutant was not more sensitive to oxidative stress or less adherent to epithelial cells as compared with the parent strain. These data suggest that this strain of A. actinomycetemcomitans has redundant systems that compensate for the MsrA activities ascribed for other organisms.

Keywords: adhesion, oxidative stress, periodontal disease

^a The GenBank accession number for the msrA sequence reported in this paper is AY026361.

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