The major outer sheath protein forms distinct conformers and multimeric complexes in the outer membrane and periplasm of Treponema denticola.

ABSTRACT: The major outer sheath protein (MOSP) is a prominent constituent of the cell envelope of Treponema denticola (TDE) and one of its principal virulence determinants. Bioinformatics predicts that MOSP consists of N- and C-terminal domains, MOSP^N and MOSP^C. Biophysical analysis of constructs refolded in vitro demonstrated that MOSP^C, previously shown to possess porin activity, forms amphiphilic trimers, while MOSP^N forms an extended hydrophilic monomer. In TDE and E. coli expressing MOSP with a PelB signal sequence (PelB-MOSP), MOSP^C is OM-embedded and surface-exposed, while MOSP^N resides in the periplasm. Immunofluorescence assay, surface proteolysis, and novel cell fractionation schemes revealed that MOSP in TDE exists as oute

SUBMITTER: Puthenveetil R 

PROVIDER: S-EPMC5643300 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature