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Infection and Immunity, May 2004, p. 2698-2702, Vol. 72, No. 5
0019-9567/04/$08.00+0 DOI: 10.1128/IAI.72.5.2698-2702.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.
Department of Restorative Dentistry and Endodontology, Osaka University Graduate School of Dentistry, Suita, Osaka 565-0871, Japan
Received 21 August 2003/ Returned for modification 10 November 2003/ Accepted 19 January 2004
Porphyromonas gingivalis, an oral bacterium, might play a role in the pathogenesis or progression of adult periodontitis. In this study, we isolated from P. gingivalis a putative glycosyltransferase gene, designated gtfA, which had a consensus domain for glycosyltransferase in its N terminus. GtfA consisted of 248 amino acids and its predicted molecular mass was 28 kDa; however, as the molecular mass of endogenous GtfA protein was around 40 kDa, this suggested that GtfA had undergone some posttranslational modifications. To reveal the role of the gtfA gene in P. gingivalis, we established gtfA-deficient strains by allelic replacement. Morphologically, gtfA-deficient P. gingivalis lacked mature fimbriae. gtfA-deficient P. gingivalis also showed a very low ability for autoaggregation, and its ability to attach to epithelial cells was severely impaired. Thus, the results indicate that the gtfA gene is required for P. gingivalis autoaggregation as well as attachment to epithelial cells. These results suggest that GtfA might have an important role in the pathogenicity of P. gingivalis by regulating adhesion.
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