Binding of bovine IgG2 a and IgG2 b allotypes to protein A, protein G, and Haemophilus somnus IgBPs
Veterinary Immunology and Immunopathology, ISSN: 0165-2427, Vol: 71, Issue: 2, Page: 143-149
1999
- 23Citations
- 20Captures
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Metrics Details
- Citations23
- Citation Indexes23
- 23
- CrossRef20
- Captures20
- Readers20
- 20
Article Description
Immunoglobulin binding proteins (IgBPs) are thought to be virulence factors which enable pathogens to evade the host’s immune response. Since bovine IgG2 is important in protection against pyogenic infections, the binding characteristics of Staphylococcus aureus protein A (PrA), streptococcal protein G (PrG), or Haemophilus somnus high molecular weight IgBPs to the two bovine IgG2 allotypes were examined. For PrA or PrG binding of IgG2, guinea pig red blood cells coated with specific IgG2 a or IgG2 b antibodies were used in a competitive binding inhibition assay with unlabeled and horseradish peroxidase-labeled PrA or PrG. To determine which sizes of H. somnus IgBPs bind to the two IgG2 allotypes, immunoblots with H. somnus culture supernatant were probed with anti-DNP IgG2 a and IgG2 b. This detects only Fc binding because anti-DNP does not cross-react with H. somnus antigens. Both IgG2 allotypes bound equally well to PrA and PrG. However, IgG2 b but not IgG2 a bound to H. somnus high molecular weight IgBPs. The lack of differential binding of bovine IgG2 allotypes to PrA and PrG means that these IgBPs can be considered to be unbiased reagents in assays for detection of bovine IgG2 or for immunoaffinity purification. The differential binding of H. somnus IgBPs to the IgG2 allotypes indicates that animals having one allotype may be more resistant to H. somnus infection than animals having the other allotype.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0165242799000926; http://dx.doi.org/10.1016/s0165-2427(99)00092-6; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0032590198&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/10532403; http://linkinghub.elsevier.com/retrieve/pii/S0165242799000926; http://api.elsevier.com/content/article/PII:S0165242799000926?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0165242799000926?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/S0165242799000926; http://dx.doi.org/10.1016/s0165-2427%2899%2900092-6; https://dx.doi.org/10.1016/s0165-2427%2899%2900092-6
Elsevier BV
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