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Glycosylation of the OMP85 homolog of Porphyromonas gingivalis and its involvement in biofilm formation |
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| Authors: | Nakao Ryoma Tashiro Yosuke Nomura Nobuhiko Kosono Saori Ochiai Kuniyasu Yonezawa Hideo Watanabe Haruo Senpuku Hidenobu |
| Institution: | a Department of Bacteriology, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Tokyo 162-8640, Japan b Graduate School of Life and Environmental Science, University of Tsukuba, Ibaraki 305-8572, Japan c Environmental Molecular Biology Laboratory, RIKEN, Saitama 351-0198, Japan d Department of Microbiology, Nihon University, Tokyo 101-8310, Japan e Department of Infectious Diseases, Kyorin University, Tokyo 181-8611, Japan |
| Abstract: | OMP85 is a highly conserved outer membrane protein in all Gram-negative bacteria. We studied an uncharacterized OMP85 homolog of Porphyromonas gingivalis, a primary periodontal pathogen forming subgingival plaque biofilms. Using an outer-loop peptide antibody specific for the OMP85 of P. gingivalis, loop-3 Ab, we found a difference in the mobility of OMP85 on SDS-PAGE gel between the P. gingivalis wild-type and the isogenic galE mutant, a deglycosylated strain, suggesting that OMP85 naturally exists in a glycosylated form. This was also supported by a shift in OMP85 PAGE mobility after chemical deglycosylation treatment. Further, loop-3 Ab cross-reacted with the galE mutant stronger than the wild-type strain; and could inhibit biofilm formation in the galE mutant more than in the wild-type strain. In conclusion, this is the first report providing the evidence of OMP85 glycosylation and the involvement of OMP85 in biofilm formation. |
| Keywords: | Porphyromonas gingivalis Gram-negative bacteria Periodontal disease OMP85 galE Glycoprotein Biofilms Glycosylation Outer membrane protein |
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