ArticleActa crystallographica. Section D, Biological crystallography2014
Schistosoma mansoni venom allergen-like protein 4 (SmVAL4) is a novel lipid-binding SCP/TAPS protein that lacks the prototypical CAP motifs.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 42 citations in OpenAlex.
- The C. elegans LON-1 protein requires its CAP domain for function in regulating body size and BMP signaling.Genetics · 2025Article
- The Proteome and Lipidome of Extracellular Vesicles fromInternational journal of molecular sciences · 2023Article
- Adaptive evolution of Moniliophthora PR-1 proteins towards its pathogenic lifestyle.BMC ecology and evolution · 2021Article
- Schistosoma mansoni venom allergen-like protein 6 (SmVAL6) maintains tegumental barrier function.International journal for parasitology · 2021Article
- The yeast cell wall protein Pry3 inhibits mating through highly conserved residues within the CAP domain.Biology open · 2020Article
- Article
- Schistosoma mansoni venom allergen-like proteins: phylogenetic relationships, stage-specific transcription and tissue localization as predictors of immunological cross-reactivity.International journal for parasitology · 2019Article
- Secreted venom allergen-like proteins of helminths: Conserved modulators of host responses in animals and plants.PLoS pathogens · 2018Review
- Venom allergen-like protein 28 in Clonorchis sinensis: four epitopes on its surface and the potential role of Cys124 for its conformational stability.Parasitology research · 2018Article
- Heligmosomoides polygyrus Venom Allergen-like Protein-4 (HpVAL-4) is a sterol binding protein.International journal for parasitology · 2018Article
- Microexon gene transcriptional profiles and evolution provide insights into blood processing by the Schistosoma japonicum esophagus.PLoS neglected tropical diseases · 2018Article
- Localization and functional characterization of the pathogenesis-related proteins Rbe1p and Rbt4p in Candida albicans.PloS one · 2018Article
- Plant pathogenesis-related proteins of the cacao fungal pathogenThe Journal of biological chemistry · 2017Article
- Crystal Structure of Borrelia turicatae protein, BTA121, a differentially regulated gene in the tick-mammalian transmission cycle of relapsing fever spirochetes.Scientific reports · 2017Article
- Tracing the Evolutionary History of the CAP Superfamily of Proteins Using Amino Acid Sequence Homology and Conservation of Splice Sites.Journal of molecular evolution · 2017Article
- Structural insights into the interaction of the conserved mammalian proteins GAPR-1 and Beclin 1, a key autophagy protein.Acta crystallographica. Section D, Structural biology · 2017Article
- Crystal Structure of MpPR-1i, a SCP/TAPS protein from Moniliophthora perniciosa, the fungus that causes Witches' Broom Disease of Cacao.Scientific reports · 2017Article
- The pathogen-related yeast protein Pry1, a member of the CAP protein superfamily, is a fatty acid-binding protein.The Journal of biological chemistry · 2017Article
- Stage and tissue expression patterns of Schistosoma mansoni venom allergen-like proteins SmVAL 4, 13, 16 and 24.Parasites & vectors · 2017Article
- Structural and functional characterization of the CAP domain of pathogen-related yeast 1 (Pry1) protein.Scientific reports · 2016Article
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Schistosomiasis is a parasitic disease that affects over 200 million people. Vaccine candidates have been identified, including Schistosoma mansoni venom allergen-like proteins (SmVALs) from the SCP/TAPS (sperm-coating protein/Tpx/antigen 5/pathogenesis related-1/Sc7) superfamily. The first SmVAL structure, SmVAL4, was refined to a resolution limit of 2.16 Å. SmVAL4 has a unique structure that could not be predicted from homologous structures, with longer loops and an unusual C-terminal extension. SmVAL4 has the characteristic α/β-sandwich and central SCP/TAPS cavity. Furthermore, SmVAL4 has only one of the signature CAP cavity tetrad amino-acid residues and is missing the histidines that coordinate divalent cations such as Zn(2+) in other SCP/TAPS proteins. SmVAL4 has a cavity between α-helices 1 and 4 that was observed to bind lipids in tablysin-15, suggesting the ability to bind lipids. Subsequently, SmVAL4 was shown to bind cholesterol in vitro. Additionally, SmVAL4 was shown to complement the in vivo sterol-export phenotype of yeast mutants lacking their endogenous CAP proteins. Expression of SmVAL4 in yeast cells lacking endogenous CAP function restores the block in sterol export. These studies suggest an evolutionarily conserved lipid-binding function shared by CAP proteins such as SmVAL4 and yeast CAP proteins such as Pry1.
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