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The Treponema Major Surface Protein is a rather large protein acting as a surface antigen in the outer sheath of Treponema denticola. It is mainly an adhesin, but it has also been showed to exhibit channel activity. The channel is estimated to have a pore diameter of 3.4 nm and prediction methods suggest that the protein possesses a transmembrane domain. Homologs are also found in other pathogenic species of Treponema. However, the ß-barrel domain may be considerably shorter than predicted, since a large portion of the N-terminal is shown to be surface-exposed and associated with antigenicity.
The major outer sheath protein of Treponema denticola inhibits the binding step of collagen phagocytosis in fibroblasts
Cell Microbiol. 2004 May;6(5):485-98. doi: 10.1111/j.1462-5822.2004.00377.x.
Pore-forming properties of the major 53-kilodalton surface antigen from the outer sheath of Treponema denticola
Infect Immun. 1993 May;61(5):1694-9. doi: 10.1128/IAI.61.5.1694-1699.1993.
Cloning and characterization of a major surface protein (MspTL) of Treponema lecithinolyticum associated with rapidly progressive periodontitis
FEMS Microbiol Lett. 2002 Feb 5;207(2):185-92. doi: 10.1111/j.1574-6968.2002.tb11049.x.
Binding properties and adhesion-mediating regions of the major sheath protein of Treponema denticola ATCC 35405
Infect Immun. 2005 May;73(5):2891-8. doi: 10.1128/IAI.73.5.2891-2898.2005.