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Home / Equine Research Bank / Immunology / Cross-antigenicity of horse serum albumin with dog and cat a...
Immunology1996; 88(3); 340-347; doi: 10.1046/j.1365-2567.1996.d01-669.x

Cross-antigenicity of horse serum albumin with dog and cat albumins: study of three short peptides with significant inhibitory activity towards specific human IgE and IgG antibodies.

Abstract: Horse serum albumin is present in the near vicinity of the animal, while dog and cat serum albumins are very common allergens present in house dust. Human patients clinically defined as allergic to horse could react with horse serum albumin by means of IgE or IgG antibodies. Studies regarding the specificities of these antibodies by inhibition enzyme-linked immunosorbent assay (ELISA) and depletion experiments have demonstrated that they are directed against dog serum albumin and cross-react not only with horse serum albumin but with other serum albumins from different origins. To investigate these observations further, we isolated and characterized three tryptic peptides (P1, P2 and P3) from horse serum albumin. The peptide P1 contains loops 1 and 2 of the first domain, P2 is derived from loop 4 of the second domain, and P3 contains the disulphide loop 9 of the third domain. These were able to inhibit the binding of the patients' IgE and IgG antibodies to horse albumin as well as to dog and cat serum albumins. This indicates that these peptides are involved in the observed cross-reactions. They also shared common epitopes, as revealed by human IgE antibodies. After reduction and alkylation, they totally lost their inhibitory capacity, suggesting that the intra-chain disulphide bridges, essential for the preservation of the loop structure, probably maintain their allergenic/antigenic reactivity.
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Publication Date: 1996-07-01 PubMed ID: 8774348PubMed Central: PMC1456354DOI: 10.1046/j.1365-2567.1996.d01-669.xGoogle Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This study investigates the cross-reactivity of horse serum albumin with dog and cat albumins, contributing to allergic reactions in humans. The authors identify three particular peptides from horse serum albumin that inhibit allergic reaction-triggering antibodies, hinting at a potential avenue for developing new treatments for allergies.

Context: Allergenic Cross-Reactivity

  • Various common allergens, including the serum albumins of horse, dog, and cat can cause allergic reactions in humans.
  • This study seeks to understand the interaction between human IgE or IgG antibodies (which play vital roles in allergic responses) and these animal albumins.
  • Earlier research suggests these antibodies primarily target dog serum albumin but also react with horse serum albumin and other albumins of different origins.

Identification of Key Peptides

  • To investigate further, the study researchers targeted three peptides, P1, P2, and P3, from horse serum albumin, each derived from different loops of the first, second, and third domains, respectively.
  • These peptides were chosen because of their presumed roles in the allergic reactions caused by animal albumins.

Peptides’ Inhibitory Effects on Allergic Responses

  • The researchers found that these peptides could inhibit the binding of IgE and IgG antibodies to horse albumin as well as dog and cat serum albumins.
  • This result underlines the role of these peptides in allergic cross-reactions and could offer the potential to block these reactions as a form of treatment.

Shared Epitopes Among Michael Peptides

  • Further analysis found common epitopes (the part of the antigen that an antibody recognizes and binds to) among the peptides, as shown by the reactions of human IgE antibodies.
  • After undergoing reduction and alkylation (chemical alterations), these peptides lost their inhibitory capabilities, suggesting that a structure maintained by disulphide bridges within the peptides plays a critical role in preserving their allergenic reactivity.

Implications of the Study

  • This study offers insights into how cross-reactive allergies function, pointing to the role of specific peptides in horse serum albumin that can block allergic responses to common allergens in pets.
  • The results could guide the development of new treatments for allergies based on inhibiting key peptides, given further testing and validation in clinical trials.

Cite This Article

APA
Goubran Botros H, Gregoire C, Rabillon J, David B, Dandeu JP. (1996). Cross-antigenicity of horse serum albumin with dog and cat albumins: study of three short peptides with significant inhibitory activity towards specific human IgE and IgG antibodies. Immunology, 88(3), 340-347. https://doi.org/10.1046/j.1365-2567.1996.d01-669.x

Publication

Immunology
ISSN: 0019-2805
NlmUniqueID: 0374672
Country: England
Language: English
Volume: 88
Issue: 3
Pages: 340-347

Researcher Affiliations

Goubran Botros, H
  • Unité d'Immuno-Allergie, Institut Pasteur, Paris, France.
Gregoire, C
    Rabillon, J
      David, B
        Dandeu, J P

          MeSH Terms

          • Allergens / immunology
          • Amino Acid Sequence
          • Animals
          • Blotting, Western
          • Cats / immunology
          • Cross Reactions
          • Dogs / immunology
          • Electrophoresis, Polyacrylamide Gel
          • Enzyme-Linked Immunosorbent Assay
          • Horses / immunology
          • Humans
          • Immunoglobulin E / immunology
          • Immunoglobulin G / immunology
          • Molecular Sequence Data
          • Serum Albumin / immunology
          • Species Specificity

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