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Members of the poorly characterized Legionella pneumophila Major Outer Membrane Protein family are proteins of around 300 amino acids in length. There is evidence that they serve as adhesive molecules for host cells, suggesting and that these proteins play a major role in the virulence of the organism. The structure is yet unknown, but prediction methods suggest that they are composed of a medium-sized ß-barrel.
Role of the 25 kDa major outer membrane protein of Legionella pneumophila in attachment to U-937 cells and its potential as a virulence factor for chick embryos
J Appl Microbiol. 1999 Feb;86(2):237-44. doi: 10.1046/j.1365-2672.1999.00667.x.
Molecular characterization of the 28- and 31-kilodalton subunits of the Legionella pneumophila major outer membrane protein
J Bacteriol. 1992 Feb;174(3):908-13. doi: 10.1128/jb.174.3.908-913.1992.
Cloning, nucleotide sequence and expression in Escherichia coli of a gene (ompM) encoding a 25 kDa major outer-membrane protein (MOMP) of legionella pneumophila
J Gen Microbiol. 1993 Aug;139(8):1715-21. doi: 10.1099/00221287-139-8-1715.
Presence in Legionella pneumophila of a mammalian-like mitochondrial permeability transition pore?
FEMS Microbiol Lett. 2008 Jan;278(2):171-6. doi: 10.1111/j.1574-6968.2007.00985.x. Epub 2007 Dec 5.