ArticleInfection and immunity2009
Glyceraldehyde-3-phosphate dehydrogenase is a surface-associated, fibronectin-binding protein of Trichomonas vaginalis.
Article in Infection and immunity, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 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
42 citing papers in PubMed, 90 citations in OpenAlex.
- Surface enolase is a virulence factor ofFrontiers in microbiology · 2026Article
- Recent Advances in Biology, Host and Microbe Interactions of the Human Sexually Transmitted ParasiteInternational journal of molecular sciences · 2025Review
- First In Silico Study of TwoInternational journal of molecular sciences · 2025Article
- An Atypical F-Actin Capping Protein Modulates Cytoskeleton Behaviors Crucial for Trichomonas vaginalis Colonization.Microbiology spectrum · 2023Article
- Point-of-Care Diagnostic forPathogens (Basel, Switzerland) · 2023Article
- The Road Less Traveled? Unconventional Protein Secretion at Parasite-Host Interfaces.Frontiers in cell and developmental biology · 2021Review
- Modulation of Rumen Microbes Through Extracellular Vesicle Released by the Rumen FlukeFrontiers in cellular and infection microbiology · 2021Article
- Chlamydia trachomatis glyceraldehyde 3-phosphate dehydrogenase: Enzyme kinetics, high-resolution crystal structure, and plasminogen binding.Protein science : a publication of the Protein Society · 2020Article
- Advancing Prevention of STIs by Developing Specific Serodiagnostic Targets:International journal of environmental research and public health · 2020Article
- Plasminogen-binding proteins as an evasion mechanism of the host's innate immunity in infectious diseases.Bioscience reports · 2018Review
- Identification ofLife science alliance · 2018Article
- Protein moonlighting: what is it, and why is it important?Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- An Alliance of Gel-Based and Gel-Free Proteomic Techniques Displays Substantial Insight Into the Proteome of a Virulent and an AttenuatedFrontiers in cellular and infection microbiology · 2018Article
- Glyceraldehyde-3-phosphate dehydrogenase acts as an adhesin in Erysipelothrix rhusiopathiae adhesion to porcine endothelial cells and as a receptor in recruitment of host fibronectin and plasminogen.Veterinary research · 2017Article
- A New Trick for a Conserved Enzyme: Mevalonate Kinase, a Glycosomal Enzyme, Can Be Secreted byFrontiers in cellular and infection microbiology · 2017Article
- Article
- The Glycolytic Enzyme Triosephosphate Isomerase of Trichomonas vaginalis Is a Surface-Associated Protein Induced by Glucose That Functions as a Laminin- and Fibronectin-Binding Protein.Infection and immunity · 2016Article
- Identification of GAPDH on the surface of Plasmodium sporozoites as a new candidate for targeting malaria liver invasion.The Journal of experimental medicine · 2016Article
- Exploiting death: apoptotic immunity in microbial pathogenesis.Cell death and differentiation · 2016Review
- Unique behavior of Trypanosoma cruzi mevalonate kinase: A conserved glycosomal enzyme involved in host cell invasion and signaling.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Trichomonas vaginalis colonizes the urogenital tract of humans and causes trichomonosis, the most prevalent nonviral sexually transmitted disease. We have shown an association of T. vaginalis with basement membrane extracellular matrix components, a property which we hypothesize is important for colonization and persistence. In this study, we identify a fibronectin (FN)-binding protein of T. vaginalis. A monoclonal antibody (MAb) from a library of hybridomas that inhibited the binding of T. vaginalis organisms to immobilized FN was identified. The MAb (called ws1) recognized a 39-kDa protein and was used to screen a cDNA expression library of T. vaginalis. A 1,086-bp reactive cDNA clone that encoded a protein of 362 amino acids with identity to glyceraldehyde-3-phosphate dehydrogenase (GAPDH) was obtained. The gapdh gene was cloned, and recombinant GAPDH (rGAPDH) was expressed in Escherichia coli cells. Natural GAPDH and rGAPDH bound to immobilized FN and to plasminogen and collagen but not to laminin. MAb ws1 inhibited binding to FN. GAPDH was detected on the surface of trichomonads and was upregulated in synthesis and surface expression by iron. Higher levels of binding to FN were seen for organisms grown in iron-replete medium than for organisms grown in iron-depleted medium. In addition, decreased synthesis of GAPDH by antisense transfection of T. vaginalis gave lower levels of organisms bound to FN and had no adverse effect on growth kinetics. Finally, GAPDH did not associate with immortalized vaginal epithelial cells (VECs), and neither GAPDH nor MAb ws1 inhibited the adherence of trichomonads to VECs. These results indicate that GAPDH is a surface-associated protein of T. vaginalis with alternative functions.
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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.