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Members of this family are Major Outer Membrane Proteins of Porphyromonas gingivalis. 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.
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.
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.