ArticlePLoS pathogens2015
A Trichomonas vaginalis Rhomboid Protease and Its Substrate Modulate Parasite Attachment and Cytolysis of Host Cells.
Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 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
36 citing papers in PubMed, 73 citations in OpenAlex.
- Study of microbe-microbe interactions between the sexually transmitted parasitebioRxiv : the preprint server for biology · 2026Article
- Trichomonas vaginalis Drug Targets and Their Role in Drug Discovery and Development.Pharmaceutical research · 2026Review
- Influence of DNA methylation and chromatin accessibility on regulation of gene expression duringmBio · 2026Article
- Recent Advances in Biology, Host and Microbe Interactions of the Human Sexually Transmitted ParasiteInternational journal of molecular sciences · 2025Review
- Host-specific targets of Histomonas meleagridis antigens revealed by immunoprecipitation.Scientific reports · 2025Article
- Iron triggersmBio · 2025Article
- TvLEGU-1 and TvLEGU-2 biomarkers for trichomoniasis are legumain-like cysteine peptidases secretedFrontiers in parasitology · 2025Article
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- PIP2 regulating calcium signal modulates actin cytoskeleton-dependent cytoadherence and cytolytic capacity in the protozoan parasite Trichomonas vaginalis.PLoS pathogens · 2023Article
- Trichomonas vaginalis adherence phenotypes and extracellular vesicles impact parasite survival in a novel in vivo model of pathogenesis.PLoS neglected tropical diseases · 2023Article
- An Atypical F-Actin Capping Protein Modulates Cytoskeleton Behaviors Crucial for Trichomonas vaginalis Colonization.Microbiology spectrum · 2023Article
- The interaction between adhesion protein 33 (TvAP33) and BNIP3 mediates the adhesion and pathogenicity of Trichomonas vaginalis to host cells.Parasites & vectors · 2023Article
- Distinct features of the host-parasite interactions between nonadherent and adherent Trichomonas vaginalis isolates.PLoS neglected tropical diseases · 2023Article
- Adherent Bacteria and Parasiticidal Secretion Products of Human Cervicovaginal Microbiota-AssociatedPharmaceuticals (Basel, Switzerland) · 2022Article
- Omics Analyses ofGenes · 2022Article
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- VPS32, a member of the ESCRT complex, modulates adherence to host cells in the parasite Trichomonas vaginalis by affecting biogenesis and cargo sorting of released extracellular vesicles.Cellular and molecular life sciences : CMLS · 2021Article
- Microparticles from human the lower airway show inhibitory activity against respiratory syncytial virus.Archives of virology · 2021Article
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Corrections and comments
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Trichomonas vaginalis is an extracellular eukaryotic parasite that causes the most common, non-viral sexually transmitted infection worldwide. Although disease burden is high, molecular mechanisms underlying T. vaginalis pathogenesis are poorly understood. Here, we identify a family of putative T. vaginalis rhomboid proteases and demonstrate catalytic activity for two, TvROM1 and TvROM3, using a heterologous cell cleavage assay. The two T. vaginalis intramembrane serine proteases display different subcellular localization and substrate specificities. TvROM1 is a cell surface membrane protein and cleaves atypical model rhomboid protease substrates, whereas TvROM3 appears to localize to the Golgi apparatus and recognizes a typical model substrate. To identify TvROM substrates, we interrogated the T. vaginalis surface proteome using both quantitative proteomic and bioinformatic approaches. Of the nine candidates identified, TVAG_166850 and TVAG_280090 were shown to be cleaved by TvROM1. Comparison of amino acid residues surrounding the predicted cleavage sites of TvROM1 substrates revealed a preference for small amino acids in the predicted transmembrane domain. Over-expression of TvROM1 increased attachment to and cytolysis of host ectocervical cells. Similarly, mutations that block the cleavage of a TvROM1 substrate lead to its accumulation on the cell surface and increased parasite adherence to host cells. Together, these data indicate a role for TvROM1 and its substrate(s) in modulating attachment to and lysis of host cells, which are key processes in T. vaginalis pathogenesis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.