ArticleClinical and experimental immunology1993
The ABA-1 allergen of the nematode Ascaris suum: epitope stability, mass spectrometry, and N-terminal sequence comparison with its homologue in Toxocara canis.
Article in Clinical and experimental immunology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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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
12 citing papers in PubMed, 40 citations in OpenAlex.
- Detection of Ascaris lumbricoides infection by ABA-1 coproantigen ELISA.PLoS neglected tropical diseases · 2020Article
- IgE Levels toFrontiers in immunology · 2020Article
- Molecular cloning and characterization of a nematode polyprotein antigen/allergen from the human and animal hookworm Ancylostoma ceylanicum.Molecular and biochemical parasitology · 2014Article
- Helminth Allergens, Parasite-Specific IgE, and Its Protective Role in Human Immunity.Frontiers in immunology · 2014Review
- Toxocara canis: molecular basis of immune recognition and evasion.Veterinary parasitology · 2013Article
- New Allergens of Relevance in Tropical Regions: The Impact of Ascaris lumbricoides Infections.The World Allergy Organization journal · 2011Article
- Characterisation of a fatty acid and retinol binding protein orthologue from the hookworm Ancylostoma ceylanicum.International journal for parasitology · 2009Article
- Association between total immunoglobulin E and antibody responses to naturally acquired Ascaris lumbricoides infection and polymorphisms of immune system-related LIG4, TNFSF13B and IRS2 genes.Clinical and experimental immunology · 2009Article
- Anisakis simplex: from obscure infectious worm to inducer of immune hypersensitivity.Clinical microbiology reviews · 2008Review
- Vaccination with an Ostertagia ostertagi polyprotein allergen protects calves against homologous challenge infection.Infection and immunity · 2004Article
- Sequence-divergent units of the ABA-1 polyprotein array of the nematode Ascaris suum have similar fatty-acid- and retinol-binding properties but different binding-site environments.The Biochemical journal · 1999Article
- Fine specificity of the genetically controlled immune response to native and recombinant gp15/400 (polyprotein allergen) of Brugia malayi.Infection and immunity · 1995Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
ABA-1 is a major allergen of nematode parasites of the genus Ascaris which includes the large roundworms of humans and pigs, A. lumbricoides and A. suum, respectively. The allergen was purified from A. suum by immunoaffinity chromatography for immunochemical examination. The IgE antibody repertoire is under MHC control in infected rodents and the IgE-binding epitopes were robust to treatment with heat or periodate, and electroblotting on nitrocellulose. This implies that the IgE epitopes comprise primary peptide sequence or an unusually stable secondary or tertiary structure. The molecular mass of ABA-1 is controversial, but mass spectrometry analysis indicated that there were five components of similar size, with the major species being 14,643.2 +/- 1.4 D. Finally, N-terminal sequence analysis of ABA-1 and TBA-1 (the homologue in the canine nematode infective to humans, Toxocara canis) revealed a high degree of similarity, and we have previous evidence that ABA-1 homologues are widespread amongst ascaridid parasites of humans. ABA-1 and its homologues might, therefore, be important to the immunopathology of many infections with nematode parasites, upon which the genetic constitution of the hosts will also have a bearing.
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