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Equine anti-hapten antibody. IX. IgM anti-lactose antibodies.

Abstract: The immune response to a bacterial vaccine of Streptococcus faecalis (strain N) was characterized in all of the seven horses studied by the sustained production of about 90% IgM anti-lactose antibody over a period of 44 weeks with maximum values of the total antibody ranging from 4 mg/ml of serum to 12 mg/ml of serum. With respect to the binding of a lactose-containing ligand the association constants of the antibodies purified from sera obtained between 5 and 44 weeks fell in the range of 1 times 10-5 M-1 to 2 times 10-5 M-1. Not only was there no significant indication of maturation of a-finity in this period but there was a selective limitation of affinity compared to that of 7S antibodies. It was inferred that the synthesis of IgM antibody involves the selective utilization of V-H and/or V-L genes.
Publication Date: 1975-01-01 PubMed ID: 803530
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  • Journal Article
  • Research Support
  • U.S. Gov't
  • P.H.S.

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 research investigates how horses respond to a bacterial vaccine by producing anti-lactose antibodies, mainly of the IgM variety. It also studies the affinity of these antibodies for lactose-containing ligands over time.

Study Summary

  • The study examines how a bacterial vaccine of Streptococcus faecalis triggers immune responses in horses. Antibody production is studied over a period of 44 weeks.
  • Specifically, the study focuses on the antibodies produced against lactose, simple sugar molecules, with a special focus on the IgM variant of these antibodies.

Findings

  • All seven horses under this study showed a sustained production of about 90% IgM anti-lactose antibodies throughout the observation period. The maximum concentration of the antibodies ranged from 4 mg/ml to 12 mg/ml of serum.
  • The researchers measured the binding strength (termed as ‘association constants’) of these antibodies to lactose-containing ligands. The recorded values varied between 1 x 10^-5 M^-1 and 2 x 10^-5 M^-1.

Analysis and Implications

  • Interestingly, over the 44 weeks period, there was no significant increase (‘maturation’) in the affinity or the binding strength of the antibodies towards lactose-containing ligands. This means the ability of the IgM antibodies to bind to lactose did not improve over time.
  • The study also points to a selective limitation in the affinity of the antibodies when compared with that of 7S antibodies, another variant.
  • The results suggest that the production of IgM antibodies involves the selective use of V-H and/or V-L genes. These genes contribute to the diversity and specificity of the antibodies.
  • Understanding such processes helps gain insights into immune response mechanisms and vaccine development in horses, and possibly in other species as well.

Cite This Article

APA
Chua MM, Morgan DO, Karush F. (1975). Equine anti-hapten antibody. IX. IgM anti-lactose antibodies. J Immunol, 114(1 Pt 1), 99-101.

Publication

ISSN: 0022-1767
NlmUniqueID: 2985117R
Country: United States
Language: English
Volume: 114
Issue: 1 Pt 1
Pages: 99-101

Researcher Affiliations

Chua, M M
    Morgan, D O
      Karush, F

        MeSH Terms

        • Adsorption
        • Animals
        • Antibodies, Heterophile / analysis
        • Antibody Formation
        • Antibody Specificity
        • Antigens, Bacterial
        • Azo Compounds
        • Carbon Radioisotopes
        • Enterococcus faecalis / immunology
        • Glycosides
        • Haptens
        • Horses / immunology
        • Immune Sera
        • Immunization Schedule
        • Immunoglobulin G
        • Immunoglobulin Heavy Chains
        • Immunoglobulin M
        • Lactose / immunology
        • Ligands
        • Polysaccharides
        • Tritium

        Citations

        This article has been cited 1 times.
        1. Allen PZ, Glode M, Schneerson R, Robbins JB. Identification of immunoglobulin heavy-chain isotypes of specific antibodies of horse 46 group B meningococcal antiserum.. J Clin Microbiol 1982 Feb;15(2):324-9.
          doi: 10.1128/jcm.15.2.324-329.1982pubmed: 6802867google scholar: lookup