OmpA-like protein influences cell shape and adhesive activity of Tannerella forsythia

被引:17
作者
Abe, T. [2 ,3 ]
Murakami, Y. [1 ,2 ]
Nagano, K. [2 ]
Hasegawa, Y. [1 ,2 ]
Moriguchi, K. [4 ]
Ohno, N. [4 ]
Shimozato, K. [3 ]
Yoshimura, F. [2 ]
机构
[1] Asahi Univ, Sch Dent, Dept Oral Microbiol, Mizuho Ku, Gifu 5010296, Japan
[2] Aichi Gakuin Univ, Sch Dent, Dept Microbiol, Nagoya, Aichi 464, Japan
[3] Aichi Gakuin Univ, Sch Dent, Dept Maxillofacial Surg, Nagoya, Aichi 464, Japan
[4] Aichi Gakuin Univ, Sch Dent, Dept Oral Anat, Nagoya, Aichi 464, Japan
基金
日本学术振兴会;
关键词
autoaggregation; bacterial adherence; cell morphology; hydrophobicity; outer membrane protein; periodontal disease; OUTER-MEMBRANE PROTEINS; ET-AL; 1986; BACTEROIDES-FORSYTHUS; PORPHYROMONAS-GINGIVALIS; ESCHERICHIA-COLI; EPITHELIAL-CELLS; IDENTIFICATION; EXPRESSION; ADHERENCE; MUTANTS;
D O I
10.1111/j.2041-1014.2011.00625.x
中图分类号
R78 [口腔科学];
学科分类号
1003 ;
摘要
Tannerella forsythia, a gram-negative fusiform rod, is implicated in several types of oral anaerobic infections. Most gram-negative bacteria have OmpA-like proteins that are homologous to the OmpA protein in Escherichia coli. We identified an OmpA-like protein in T. forsythia encoded by the tf1331 gene as one of the major proteins by mass spectrometric analysis. Two-dimensional, diagonal electrophoresis showed that the OmpA-like protein formed a dimeric or trimeric structure via intermolecular disulfide bonds. A biotin labeling experiment revealed that a portion of the protein was exposed on the cell surface, even though T. forsythia possesses an S-layer at the outermost cell surface. Using a tf1331-deletion mutant, we showed that the OmpA-like protein affected cell morphology. The length of the mutant cell was reduced almost by half. Cell swelling was observed in more than 40% of the mutant cells. Moreover, the mutant exhibited decreased adhesion to fibronectin, retarded autoaggregation, and reduced cell surface hydrophobicity. These results suggest that the OmpA-like protein in T. forsythia plays an important role in cellular integrity and adhesive function.
引用
收藏
页码:374 / 387
页数:14
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