ArticleMolecular and biochemical parasitology2014
Molecular cloning and characterization of a nematode polyprotein antigen/allergen from the human and animal hookworm Ancylostoma ceylanicum.
Article in Molecular and biochemical parasitology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 11 citations in OpenAlex.
- Characterization and ligand binding properties of a fatty acid- and retinol- binding protein (Hp-FAR-2) from Heligmosomoides polygyrus.PLoS neglected tropical diseases · 2025Article
- A secreted fatty acid- and retinol- binding protein frombioRxiv : the preprint server for biology · 2025Article
- Excretory/Secretory Proteome of Females and Males of the HookwormPathogens (Basel, Switzerland) · 2023Article
- The FAR protein family of parasitic nematodes.PLoS pathogens · 2022Review
- Parasitic nematode fatty acid- and retinol-binding proteins compromise host immunity by interfering with host lipid signaling pathways.PLoS pathogens · 2021Article
- Mining nematode protein secretomes to explain lifestyle and host specificity.PLoS neglected tropical diseases · 2021Article
- Twenty-five-year research progress in hookworm excretory/secretory products.Parasites & vectors · 2020Review
- Fatty acid and retinol-binding protein: A novel antigen for immunodiagnosis of human strongyloidiasis.PloS one · 2019Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Nematodes are unable to synthesize fatty acids de novo and must acquire them from the environment or host. It is hypothesized that two unique classes of fatty acid and retinol binding proteins that nematodes produce (fatty acid and retinol binding (FAR) and nematode polyprotein antigen/allergen (NPA)) are used to meet this need. A partial cDNA has been cloned corresponding to four subunits of a putative Ancylostoma ceylanicum NPA (AceNPA). The translated amino acid sequence of AceNPA shares sequence identity with similar proteins from Dictyocaulus viviparus, Ascaris suum, and Ostertagia ostertagi. Immunoblot experiments using a polyclonal anti-AceNPA IgG revealed proteins corresponding to the expected sizes of single, as well as two or three un-cleaved NPA subunits in adult excretory/secretory proteins and soluble adult worm extracts. Immunohistochemistry experiments localize AceNPA to the cuticle, pseudocoelomic space and testes suggesting a role in hookworm biology that is distinct from what has previously been defined for other hookworm lipid binding proteins. A single recombinant subunit of AceNPA (rAceNPAb) demonstrated binding in vitro to fluorescent fatty acids DAUDA, cis-parinaric acid, as well as retinol, at equilibrium dissociation constants in the low micromolar range. Further, in vitro data reveal that rAceNPAb binds fatty acids with chain lengths of C12-C22, with the greatest affinities for arachidonic, linoleic (C18), and eicosapentaenoic (C20) acids.
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