Cloning and sequencing of the equine and ovine high-affinity IgE receptor beta-and gamma-chain cDNA.
Abstract: The high-affinity receptor for IgE is expressed on the surface of mast cells and basophils. It is a transmembrane protein with one alpha, one beta and two gamma subunits. The cDNA sequences for the alpha subunit have already been determined. We report here the cDNA sequences for the beta and gamma subunits. The cytoplasmic domains of these subunits are important for intracellular signalling and the deduced amino acid sequences show the expected immunoreceptor tyrosine-based activation motifs. The gamma subunit is highly conserved between species but more variation is seen with the beta subunit. Near the C terminus of the equine beta chain there is a two-base deletion, which changes the reading frame: residue 237 (human numbering) becomes Asp instead of Glu and the chain is three amino acids shorter than the other known mammalian and rodent sequences.
Publication Date: 2003-04-23 PubMed ID: 12709836DOI: 10.1007/s00251-003-0564-yGoogle Scholar: Lookup
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- Journal Article
- Research Support
- Non-U.S. Gov't
Summary
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This study explores the genetic sequences for the beta and gamma subunits of the high-affinity receptor for IgE present on the surface of mast cells and basophils in horses and sheep.
Background of Study
- The research centers on the high-affinity receptor for IgE, which is a transmembrane protein found on the surface of mast cells and basophils.
- This receptor is made up of one alpha, one beta, and two gamma subunits. The genetic sequences for the alpha subunit were already known, so this study focuses on the beta and gamma subunits.
Research Methodology
- The researchers cloned and sequenced the cDNA (complementary DNA) sequences for the beta and gamma subunits of the high-affinity receptor for IgE.
- These subunits are significant because their cytoplasmic domains play a vital role in intracellular signaling.
- The deduced amino acid sequences were checked for anticipated immunoreceptor tyrosine-based activation motifs.
Key Findings
- Findings revealed that the gamma subunit is highly conserved across different species. This implies that the gamma subunit’s structure and function have remained relatively stable throughout evolutionary history due to its biological significance.
- On the other hand, researchers observed more variation in the beta subunit when compared to the gamma subunit, suggesting adaptive modification and evolution over time.
- A unique feature was found in the equine beta chain near its C terminus, where a two-base deletion changed the reading frame. The 237th residue (using human numbering for comparison) changes from Glu (glutamic acid) to Asp (aspartic acid), making the chain three amino acids shorter than other known mammalian and rodent sequences.
Implications of Research
- This study’s findings contribute to the overall scientific understanding of the structure and function of the high-affinity IgE receptor.
- Such information can be valuable for further research into the role of this receptor in health and disease, potentially providing insights for the development of new treatments for conditions which involve the immune system.
Cite This Article
APA
McAleese SM, Miller HR.
(2003).
Cloning and sequencing of the equine and ovine high-affinity IgE receptor beta-and gamma-chain cDNA.
Immunogenetics, 55(2), 122-125.
https://doi.org/10.1007/s00251-003-0564-y Publication
Researcher Affiliations
- Department of Veterinary Clinical Studies, R(D)SVS, Easter Bush Veterinary Centre, University of Edinburgh, EH25 9RG, Roslin, Midlothian, UK. smm@vet.ed.ac.uk
MeSH Terms
- Amino Acid Sequence
- Animals
- Base Sequence
- DNA, Complementary
- Horses / genetics
- Molecular Sequence Data
- Receptors, IgE / genetics
- Sheep / genetics
References
This article includes 17 references
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Citations
This article has been cited 3 times.- Larson EM, Babasyan S, Wagner B. Phenotype and function of IgE-binding monocytes in equine Culicoides hypersensitivity. PLoS One 2020;15(5):e0233537.
- Eon Kuek L, Leffler M, Mackay GA, Hulett MD. The MS4A family: counting past 1, 2 and 3. Immunol Cell Biol 2016 Jan;94(1):11-23.
- Qiao S, Yang Y, Liu Y, Zhang G, Xi J, Zhang H, Hao H, Tian X, Yang S, Deng R. Characterization and ligand specificity of sheep IgG2 receptor. Immunogenetics 2009 Aug;61(8):597-601.
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