ArticleThe Journal of biological chemistry2014
Solution structure, membrane interactions, and protein binding partners of the tetraspanin Sm-TSP-2, a vaccine antigen from the human blood fluke Schistosoma mansoni.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 44 citations in OpenAlex.
- Trial
- mRNA vaccines encoding variant forms of Sm-TSP-2 confer protective immunity against Schistosoma mansoni.NPJ vaccines · 2025Article
- Molecular characterization and B-cell epitope analysis of the TSP11 gene inParasitology · 2024Article
- Progress on the Regulation of the Host Immune Response by Parasite-Derived Exosomes.Pathogens (Basel, Switzerland) · 2024Review
- Tetraspanins: structure, dynamics, and principles of partner-protein recognition.Trends in cell biology · 2024Review
- Human growth factor-mediated signalling through lipid rafts regulates stem cell proliferation, development and survival ofOpen biology · 2024Article
- Can antibody conjugated nanomicelles alter the prospect of antibody targeted therapy against schistosomiasis mansoni?PLoS neglected tropical diseases · 2023Article
- Schistosoma mansoni excretory-secretory products induce protein kinase signalling, hyperkinesia, and stem cell proliferation in the opposite sex.Communications biology · 2023Article
- Advances in new target molecules against schistosomiasis: A comprehensive discussion of physiological structure and nutrient intake.PLoS pathogens · 2023Review
- A Critical Review on Human Malaria and Schistosomiasis Vaccines: Current State, Recent Advancements, and Developments.Vaccines · 2023Review
- Optimization of Expression and Purification of Schistosoma mansoni Antigens in Fusion with Rhizavidin.Molecular biotechnology · 2021Article
- Recent Advances and Methodological Considerations on Vaccine Candidates for Human Schistosomiasis.Frontiers in tropical diseases · 2021Article
- Natural Intra- and Interclade Human Hybrid Schistosomes in Africa with Considerations on Prevention through Vaccination.Microorganisms · 2021Review
- Primary and Memory Response of Human Monocytes to Vaccines: Role of Nanoparticulate Antigens in Inducing Innate Memory.Nanomaterials (Basel, Switzerland) · 2021Article
- Human serum activates the tegument of female schistosomes and supports recovery from Praziquantel.Parasitology research · 2021Article
- Open conformation of tetraspanins shapes interaction partner networks on cell membranes.The EMBO journal · 2020Article
- High Yield Expression of Recombinant CD151 in E. coli and a Structural Insight into Cholesterol Binding Domain.Molecular biotechnology · 2019Article
- Gene Expression in Developmental Stages ofInternational journal of molecular sciences · 2019Article
- Glucose Uptake in the Human Pathogen Schistosoma mansoni Is Regulated Through Akt/Protein Kinase B Signaling.The Journal of infectious diseases · 2018Article
- Suppression of mRNAs encoding CD63 family tetraspanins from the carcinogenic liver fluke Opisthorchis viverrini results in distinct tegument phenotypes.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
13 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The tetraspanins (TSPs) are a family of integral membrane proteins that are ubiquitously expressed at the surface of eukaryotic cells. TSPs mediate a range of processes at the surface of the plasma membrane by providing a scaffold for the assembly of protein complexes known as tetraspanin-enriched microdomains (TEMs). We report here the structure of the surface-exposed EC2 domain from Sm-TSP-2, a TSP from Schistosoma mansoni and one of the better prospects for the development of a vaccine against schistosomiasis. This is the first solution structure of this domain, and our investigations of its interactions with lipid micelles provide a general model for interactions between TSPs, membranes, and other proteins. Using chemical cross-linking, eight potential protein constituents of Sm-TSP-2-mediated TEMs were also identified. These include proteins important for membrane maintenance and repair, providing further evidence for the functional role of Sm-TSP-2- and Sm-TSP-2-mediated TEMs. The identification of calpain, Sm29, and fructose-bisphosphate aldolase, themselves potential vaccine antigens, suggests that the Sm-TSP-2-mediated TEMs could be disrupted via multiple targets. The identification of further Sm-TSP-2-mediated TEM proteins increases the available candidates for multiplex vaccines and/or novel drugs targeting TEMs in the schistosome tegument.
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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.