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Analysis of horse serum inhibitors of A2 influenza virus haemagglutination.

Abstract: No abstract available
Publication Date: 1965-10-01 PubMed ID: 4158312PubMed Central: PMC2094621
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  • Journal Article

Summary

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The research article presents an analysis of horse serum inhibitors that affect the hemagglutination of the A2 influenza virus strains. The article dives into the molecular nature of these inhibitors, looking specifically at differences in the protein fractions carrying this inhibitory activity in regular and atypical horse sera.

Identifying the Inhibitors

  • The authors are discussing a particular type of haemagglutination inhibitor, named as γ-inhibitor, found in horse and guinea-pig serum. Besides, they acknowledge the existence of other types of inhibitors, referred to as o- and /-types. Moreover, some horse sera display inhibitory properties similar to the αχ-type, and these sera are labeled as atypical.
  • Haemagglutination inhibitors can prevent the clumping of red blood cells, a process often initiated by certain viruses, including influenza.
  • The γ-inhibitor identified is mostly effective against A2 strains of influenza virus.

Molecular Nature of the Inhibitors

  • Through treatment with periodate and trypsin, the research team found that the inhibitory activity in both γ-inhibitory and atypical horse sera is mediated by substances of mucoprotein nature. Mucoproteins are proteins linked to carbohydrates, which could have a vital role in immune responses.
  • The inhibitors found in atypical sera were found susceptible to inactivation by neuraminidase, a type of enzyme. This suggests that one of the main chemical differences between the atypical and γ-inhibitors lies in the carbohydrate prosthetic groups of the inhibitory mucoprotein molecules.

Serum Protein Fractions Carrying Inhibitory Activity

  • The research then shifted to identify which serum protein fractions carried the inhibitory activity in both regular and atypical horse sera.
  • Initial attempts involved using a technique known as “salting out” with ammonium sulphate to separate the active serum fractions.
  • No marked difference in the pattern of inhibitor distribution in the two types of serum was found with this initial method.

Comparisons with Other Research

  • The article also compares the findings with previous researches from other authors who used different fractionation methods, identifying activity in a narrower range of components and its absence from γ-globulin.
  • The findings provide insights into the complex nature of viruses and how different organisms respond to them at the molecular level, which could open new paths of investigation in the development of antiviral treatments.

Cite This Article

APA
Cohen A, Biddle F, Newland SE. (1965). Analysis of horse serum inhibitors of A2 influenza virus haemagglutination. Br J Exp Pathol, 46(5), 497-513.

Publication

ISSN: 0007-1021
NlmUniqueID: 0372543
Country: England
Language: English
Volume: 46
Issue: 5
Pages: 497-513

Researcher Affiliations

Cohen, A
    Biddle, F
      Newland, S E

        MeSH Terms

        • Animals
        • Blood Protein Electrophoresis
        • Chromatography, Ion Exchange
        • Hemagglutination
        • Hemagglutination Inhibition Tests
        • Horses
        • Immune Sera
        • In Vitro Techniques
        • Mucoproteins
        • Neuraminidase
        • Nitrogen
        • Orthomyxoviridae / immunology
        • Quaternary Ammonium Compounds
        • gamma-Globulins

        References

        This article includes 11 references
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        Citations

        This article has been cited 2 times.
        1. Kang YP, Ward NP, DeNicola GM. Recent advances in cancer metabolism: a technological perspective. Exp Mol Med 2018 Apr 16;50(4):1-16.
          doi: 10.1038/s12276-018-0027-zpubmed: 29657324google scholar: lookup
        2. Lukert PD. Avian infectious bronchitis virus characteristics of an inhibitor found in serum. Arch Gesamte Virusforsch 1973;40(1):93-104.
          doi: 10.1007/BF01242641pubmed: 4120845google scholar: lookup