ArticleMolecular oral microbiology2025
Topology and functional characterization of major outer membrane proteins of Treponema maltophilum and Treponema lecithinolyticum.
Article in Molecular oral microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- Neutrophil-Derived Oncostatin M Contributes to Endothelial Cell Dysfunction DuringbioRxiv : the preprint server for biology · 2026Article
- Genetic predictive links between oropharyngeal microecology and obstructive sleep apnea syndrome: expanding the perspective of etiology.Journal of oral microbiology · 2026Review
- Neutrophil-derived oncostatin m contributes to endothelial cell dysfunction during Treponema denticola interaction.PloS one · 2026Article
- Emerging oralFrontiers in oral health · 2025Article
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Authors and funding
9 authors.
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Abstract
Numerous Treponema species are prevalent in the dysbiotic subgingival microbial community during periodontitis. The major outer sheath protein is a highly expressed virulence factor of the well-characterized species Treponema denticola. Msp forms an oligomeric membrane protein complex with adhesin and porin properties and contributes to host-microbial interaction. Treponema maltophilum and Treponema lecithinolyticum species are also prominent during periodontitis but are relatively understudied. Msp-like membrane surface proteins exist in T. maltophilum (MspA) and T. lecithinolyticum (MspTL), but limited information exists regarding their structural features or functionality. Protein profiling reveals numerous differences between these species, but minimal differences between strains of the same species. Using protein modeling tools, we predict MspA and MspTL monomeric forms to be large β-barrel structures composed of 20 all-next-neighbor antiparallel β strands which most likely adopt a homotrimer formation. Using cell fractionation, Triton X-114 phase partitioning, heat modifiability, and chemical and detergent release assays, we found evidence of amphiphilic integral membrane-associated oligomerization for both native MspA and MspTL in intact spirochetes. Proteinase K accessibility and immunofluorescence assays demonstrate surface exposure of MspA and MspTL. Functionally, purified recombinant MspA or MspTL monomer proteins can impair neutrophil chemotaxis. Expressions of MspA or MspTL with a PelB leader sequence in Escherichia coli also demonstrate surface exposure and can impair neutrophil chemotaxis in an in vivo air pouch model of inflammation. Collectively, our data demonstrate that MspA and MspTL membrane proteins can contribute to pathogenesis of these understudied oral spirochete species.
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