ArticleImmunology1990
N-terminal amino acid sequence identity between a major allergen of Ascaris lumbricoides and Ascaris suum, and MHC-restricted IgE responses to it.
Article in Immunology, 1990. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 59 citations in OpenAlex.
- The liver proteome in a mouse model for Ascaris suum resistance and susceptibility: evidence for an altered innate immune response.Parasites & vectors · 2019Article
- Immunomodulation of liver injury by Ascaris suum extract in an experimental model of autoimmune hepatitis.Parasitology research · 2014Article
- New Allergens of Relevance in Tropical Regions: The Impact of Ascaris lumbricoides Infections.The World Allergy Organization journal · 2011Article
- Isolation of a heat-resistant allergen from the fish parasite Anisakis simplex.Parasitology research · 2005Article
- The polyprotein and FAR lipid binding proteins of nematodes: shape and monomer/dimer states in ligand-free and bound forms.European biophysics journal : EBJ · 2003Article
- 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
- Novel classes of fatty acid and retinol binding protein from nematodes.Molecular and cellular biochemistry · 1999Review
- Differential antibody isotype reactivity to specific antigens in human lymphatic filariasis: gp15/400 preferentially induces immunoglobulin E (IgE), IgG4, and IgG2.Infection and immunity · 1995Article
- Allergen nomenclature. IUIS/WHO Allergen Nomenclature Subcommittee.Bulletin of the World Health Organization · 1994Article
- Primary structure of and immunoglobulin E response to the repeat subunit of gp15/400 from human lymphatic filarial parasites.Infection and immunity · 1993Article
- The ABA-1 allergen of the nematode Ascaris suum: epitope stability, mass spectrometry, and N-terminal sequence comparison with its homologue in Toxocara canis.Clinical and experimental immunology · 1993Article
- Cloning of a cuticular antigen that contains multiple tandem repeats from the filarial parasite Dirofilaria immitis.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
- MHC class II (I-A) region control of the IgE antibody repertoire to the ABA-1 allergen of the nematode Ascaris.Immunology · 1991Article
- IgE antibody production in rats against multiple components of excretory-secretory products of the nematode Nippostrongylus brasiliensis.Immunology · 1991Article
- MHC (RT1) restriction of the antibody repertoire to infection with the nematode Nippostrongylus brasiliensis in the rat.Immunology · 1990Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
A protein allergen of the parasitic nematode Ascaris has been purified to homogeneity by immunoaffinity chromatography. It is the most abundant protein species in the parasite's body fluid and has been named ABA-1. The allergen's molecular weight (MW) has been previously estimated at 14,000, but this sizing is currently under re-evaluation. The immunological activity of the protein was intact after purification, as attested by immunoprecipitation and passive cutaneous anaphylaxis. The IgE response to ABA-1 was under major histocompatibility complex (MHC) restriction in the rat, in which only RT1u strains were found to respond following infection with the parasite. The tissue-invasive and intestinal stages of both Ascaris lumbricoides (of humans) and Ascaris suum (of pigs) have an antigen of similar MW to ABA-1 in their secretions or among their somatic antigens. These are antigenically indistinguishable; they were found to have similar amino acid compositions, and their N-terminal amino acid sequences were identical to 41 residues. Finally, the apparent MW, amino acid composition and isoelectric point of ABA-1 all argue for close similarity to the previously described Allergen A of the parasite.
Indexed as
Identifiers
2335378PMC1385635W313247338What OpenQuestion holds
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.