Glycosylation of the OMP85 homolog of Porphyromonas gingivalis and its involvement in biofilm formation.
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.
Nakao
Ryoma
R
Department of Bacteriology, National Institute of Infectious Diseases, 1-23-1 Toyama, Shinjuku-ku, Tokyo 162-8640, Japan.
Tashiro
Yosuke
Y
Nomura
Nobuhiko
N
Kosono
Saori
S
Ochiai
Kuniyasu
K
Yonezawa
Hideo
H
Watanabe
Haruo
H
Senpuku
Hidenobu
H
D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism*; D018441:Biofilms / Q000254:growth & development*; D049109:Cell Proliferation; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D006031:Glycosylation; D016966:Porphyromonas gingivalis / Q000254:growth & development* / Q000378:metabolism*
D001425:Bacterial Outer Membrane Proteins; C503914:BamA protein, E coli; D029968:Escherichia coli Proteins