ArticleInternational journal for parasitology2018
Heligmosomoides polygyrus Venom Allergen-like Protein-4 (HpVAL-4) is a sterol binding protein.
Article in International journal for parasitology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 30 citations in OpenAlex.
- Article
- The C. elegans LON-1 protein requires its CAP domain for function in regulating body size and BMP signaling.Genetics · 2025Article
- Loss of Sterol Biosynthesis in Economically Important Plant Pests and Pathogens: A Review of a Potential Target for Pest Control.Biomolecules · 2024Review
- Cymbopogon citratus showing nematicidal activity against Heligmosomoides polygyrus bakeri.Revista brasileira de parasitologia veterinaria = Brazilian journal of veterinary parasitology : Orgao Oficial do Colegio Brasileiro de Parasitologia Veterinaria · 2024Article
- Plant-based production of a protective vaccine antigen against the bovine parasitic nematode Ostertagia ostertagi.Scientific reports · 2023Article
- A member of the CAP protein superfamily, Hc-CAP-15, is important for the parasitic-stage development of Haemonchus contortus.Parasites & vectors · 2023Article
- The Proteome and Lipidome of Extracellular Vesicles fromInternational journal of molecular sciences · 2023Article
- Novel antiinflammatory biologics shaped by parasite-host coevolution.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A filarial parasite-encoded human IL-10 receptor antagonist reveals a novel strategy to modulate host responses.PNAS nexus · 2022Article
- β-Hexosaminidases Along the Secretory Pathway ofFrontiers in plant science · 2021Article
- Article
- The Two Faces of Nematode Infection: Virulence and Immunomodulatory Molecules From Nematode Parasites of Mammals, Insects and Plants.Frontiers in microbiology · 2020Review
- The Gastrointestinal HelminthFrontiers in immunology · 2020Article
- Secreted venom allergen-like proteins of helminths: Conserved modulators of host responses in animals and plants.PLoS pathogens · 2018Review
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Authors and funding
10 authors at 4 institutions in 4 countries.
Funding
Abstract
Heligmosomoides polygyrus bakeri is a model parasitic hookworm used to study animal and human helminth diseases. During infection, the parasite releases excretory/secretory products that modulate the immune system of the host. The most abundant protein family in excretory/secretory products comprises the venom allergen-like proteins (VALs), which are members of the SCP/TAPS (sperm-coating protein/Tpx/antigen 5/pathogenesis related-1/Sc7) superfamily. There are >30 secreted Heligmosomoides polygyrus VAL proteins (HpVALs) and these proteins are characterised by having either one or two 15 kDa CAP (cysteine-rich secretory protein (CRISP)/antigen 5/pathogenesis related-1) domains. The first known HpVAL structure, HpVAL-4, refined to 1.9 Å is reported. HpVAL-4 was produced as a homogeneously glycosylated protein in leaves of Nicotiana benthamiana infiltrated with recombinant plasmids, making this plant expression platform amenable for the production of biological products. The overall topology of HpVAL-4 is a three layered αβα sandwich between a short N-terminal loop and a C-terminal cysteine rich extension. The C-terminal cysteine rich extension has two strands stabilized by two disulfide bonds and superposes well with the previously reported extension from the human hookworm Necator americanus Ancylostoma secreted protein-2 (Na-ASP-2). The N-terminal loop is connected to alpha helix 2 via a disulfide bond previously observed in Na-ASP-2. HpVAL-4 has a central cavity that is more similar to the N-terminal CAP domain of the two CAP Na-ASP-1 from Necator americanus. Unlike Na-ASP-2, mammalian CRISP, and the C-terminal CAP domain of Na-ASP-1, the large central cavity of HpVAL-4 lacks the two histidines required to coordinate divalent cations. HpVAL-4 has both palmitate-binding and sterol-binding cavities and is able to complement the in vivo sterol export phenotype of yeast mutants lacking their endogenous CAP proteins. More studies are required to determine endogenous binding partners of HpVAL-4 and unravel the possible impact of sterol binding on immune-modulatory functions.
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