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Journal of Bacteriology, October 2001, p. 5645-5650, Vol. 183, No. 19
Department of Microbiology, The University of
Texas Health Science Center at San Antonio, San Antonio, Texas
78229
Received 13 April 2001/Accepted 11 July 2001
Mycoplasma genitalium is the smallest
self-replicating microorganism and is implicated in human
diseases, including urogenital and respiratory infections and
arthritides. M. genitalium colonizes host cells primarily
through adherence mechanisms mediated by a network of
surface-associated membrane proteins, including adhesins and
cytadherence-related proteins. In this paper, we show that cytadherence
in M. genitalium is affected by an unrelated protein known
as peptide methionine sulfoxide reductase (MsrA), an antioxidant repair
enzyme that catalyzes the reduction of methionine sulfoxide [Met(O)]
residues in proteins to methionine. An msrA disruption mutant of M. genitalium, constructed through homologous
recombination, displayed markedly reduced adherence to sheep
erythrocytes. In addition, the msrA mutant was incapable of
growing in hamsters and exhibited hypersensitivity to hydrogen peroxide
when compared to wild-type virulent M. genitalium. These
results indicate that MsrA plays an important role in M. genitalium pathogenicity, possibly by protecting mycoplasma
protein structures from oxidative damage or through alternate
virulence-related pathways.
0021-9193/01/$04.00+0 DOI: 10.1128/JB.183.19.5645-5650.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.
Peptide Methionine Sulfoxide Reductase (MsrA) Is a
Virulence Determinant in Mycoplasma genitalium
*
Corresponding author. Mailing address: Department of
Microbiology, The University of Texas Health Science Center at San
Antonio, 7703 Floyd Curl Dr., San Antonio, TX 78229. Phone: (210)
567-3939. Fax: (210) 567-6612. E-mail: baseman{at}uthscsa.edu.
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