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Veterinary immunology and immunopathology2005; 108(1-2); 139-143; doi: 10.1016/j.vetimm.2005.07.008

IgA Fc receptors in cattle and horses.

Abstract: The biological role of IgA depends, at least partly, on the interaction with specific receptors (FcalphaRs) on the surface of leukocytes. The human FcalphaR, CD89, was the first IgA Fc receptor to be identified, and binding of IgA-coated particles to CD89 triggers numerous cellular effector functions including phagocytosis, antibody-dependent cell-mediated cytotoxicity (ADCC), and release of inflammatory mediators. Recently, CD89 orthologs have been identified in a number of other species, including cows and horses. This brief review will summarize our current knowledge regarding the structure and function of bovine and equine CD89.
Publication Date: 2005-08-16 PubMed ID: 16098605DOI: 10.1016/j.vetimm.2005.07.008Google Scholar: Lookup
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  • Comparative Study
  • Journal Article
  • Review

Summary

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The research aims to understand the role and behaviour of IgA Fc receptors, specifically the CD89 receptor, in cattle and horses as it affects the performance of leukocytes involved in the immune response.

Understanding FcalphaRs

  • The focus of the paper is on IgA Fc receptors (FcalphaRs), which are found on the surface of leukocytes, or white blood cells. Their role in the biological performance of IgA, a type of antibody, is highlighted.
  • The interaction between IgA-coated particles and these FcalphaRs play a crucial role in the immune response. This interaction triggers numerous cellular effector functions such as phagocytosis – the process by which cells ingest harmful particles or bacteria, antibody-dependent cell-mediated cytotoxicity (ADCC) – a process that enables cells to kill target cells, and the release of inflammatory mediators that help to combat infections.

CD89 Receptor

  • The CD89 receptor, a subtype of the IgA Fc receptor, is primarily discussed in the study. This receptor was the first IgA Fc receptor to be identified in humans.
  • As mentioned, the CD89 receptor plays a role in instigating cellular actions such as phagocytosis, ADCC, and the release of inflammatory mediators when it binds with IgA-coated particles. Therefore, it plays a critical role in the immune system’s defense mechanisms.

CD89 Orthologs in Other Species

  • Coupled with the exploration of the human CD89 receptor is the comparison with its orthologs – equivalent receptors in different species – specifically in cows and horses.
  • The CD89 orthologs have only recently been identified in some animal species, including cows and horses, suggesting they also play a role in the immune response of these animals.
  • It is therefore anticipated that understanding these orthologs can provide unique insight into the structure and function of CD89 receptors, and consequently, the broader immune response.

Objective of Research

  • The research seeks to extend our understanding of the structure and function of bovine and equine CD89, thus contributing further knowledge to the field of immunology, particularly in relation to livestock and equine health.

Cite This Article

APA
Morton HC. (2005). IgA Fc receptors in cattle and horses. Vet Immunol Immunopathol, 108(1-2), 139-143. https://doi.org/10.1016/j.vetimm.2005.07.008

Publication

ISSN: 0165-2427
NlmUniqueID: 8002006
Country: Netherlands
Language: English
Volume: 108
Issue: 1-2
Pages: 139-143

Researcher Affiliations

Morton, H Craig
  • Laboratory for Immunohistochemistry and Immunopathology (LIIPAT), Institute of Pathology, Rikshospitalet University Hospital, N-0027 Oslo, Norway.. h.c.morton@medisin.uio.no

MeSH Terms

  • Amino Acid Sequence
  • Animals
  • Antigens, CD / chemistry
  • Antigens, CD / genetics
  • Antigens, CD / metabolism
  • Cattle / genetics
  • Cattle / immunology
  • Horses / genetics
  • Horses / immunology
  • Humans
  • Immunoglobulin A / metabolism
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Receptors, Fc / chemistry
  • Receptors, Fc / genetics
  • Receptors, Fc / metabolism
  • Sequence Homology, Amino Acid
  • Species Specificity

Citations

This article has been cited 2 times.
  1. Bakema JE, van Egmond M. Immunoglobulin A: A next generation of therapeutic antibodies?. MAbs 2011 Jul-Aug;3(4):352-61.
    doi: 10.4161/mabs.3.4.16092pubmed: 21691145google scholar: lookup
  2. Parham P. The genetic and evolutionary balances in human NK cell receptor diversity.. Semin Immunol 2008 Dec;20(6):311-6.
    doi: 10.1016/j.smim.2008.10.002pubmed: 19036608google scholar: lookup