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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 outer membrane (OM) and periplasmic trimeric conformers; PelB-MOSP, in contrast, formed only OM-MOSP trimers. Although both conformers form hetero-oligomeric complexes in TDE, only OM-MOSP associates with dentilisin. Mass spectrometry (MS) indicated that OM-MOSP interacts with proteins in addition to dentilisin, most notably, oligopeptide-binding proteins (OBPs) and the β-barrel of BamA. MS also identified candidate partners for periplasmic MOSP, including TDE1658, a spirochete-specific SurA/PrsA ortholog. Collectively, our data suggest that MOSP destined for the TDE OM follows the canonical BAM pathway, while formation of a stable periplasmic conformer involves an export-related, folding pathway not present in  E. coli .

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