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Members of this family are Major Outer Membrane Proteins of Porphyromonas gingivalis. Porphyromonas gingivalis possesses various abilities to evade and disrupt host immune responses, by which it acts as an important periodontal pathogen. P. gingivalis produces outer membrane protein A (OmpA)-like proteins (OmpALPs), Pgm6 and Pgm7, as major O-linked glycoproteins. They resemble members of the OmpA family in their C-terminal domain that protrudes in the periplasmic space. The N-terminal membrane anchor domain though does not show any significant sequence similarity. Two-dimensional, diagonal electrophoresis and chemical cross-linking experiments with or without a reducing agent clearly showed that these proteins mainly form stable heterotrimers via intermolecular disulfide bonds. It has been suggested that they play an important role in the integrity of the outer membrane and, similar to members of the Ompa family, are likely to function as a stabilizer of the cell wall rather than as a major porin in this organism.
OmpA-like proteins of Porphyromonas gingivalis contribute to serum resistance and prevent Toll-like receptor 4-mediated host cell activation
PLoS One. 2018 Aug 28;13(8):e0202791. doi: 10.1371/journal.pone.0202791. eCollection 2018.
Characterization of wheat germ agglutinin lectin-reactive glycosylated OmpA-like proteins derived from Porphyromonas gingivalis
Infect Immun. 2014 Nov;82(11):4563-71. doi: 10.1128/IAI.02069-14. Epub 2014 Aug 18.
Identification and characterization of novel glycoproteins involved in growth and biofilm formation by Porphyromonas gingivalis
Mol Oral Microbiol. 2012 Dec;27(6):458-70. doi: 10.1111/j.2041-1014.2012.00659.x. Epub 2012 Jul 21.
E-selectin mediates Porphyromonas gingivalis adherence to human endothelial cells
Infect Immun. 2012 Jul;80(7):2570-6. doi: 10.1128/IAI.06098-11. Epub 2012 Apr 16.
Trimeric structure of major outer membrane proteins homologous to OmpA in Porphyromonas gingivalis
J Bacteriol. 2005 Feb;187(3):902-11. doi: 10.1128/JB.187.3.902-911.2005.
Characterization of two outer membrane protein antigens of Porphyromonas gingivalis that are protective in a murine lesion model
Oral Microbiol Immunol. 2004 Feb;19(1):6-15. doi: 10.1046/j.0902-0055.2003.00096.x.