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Home / Equine Research Bank / J Gen Virol / Intracellular proteins of feline immunodeficiency virus and ...
The Journal of general virology1990; 71 ( Pt 3); 739-743; doi: 10.1099/0022-1317-71-3-739

Intracellular proteins of feline immunodeficiency virus and their antigenic relationship with equine infectious anaemia virus proteins.

Abstract: Feline immunodeficiency virus (FIV) grown in cat lymphocyte and thymocyte cultures was labelled with L-[35S]methionine or [3H]glucosamine and virus-coded proteins were identified using immunoprecipitation. Polypeptides with apparent Mr values of 15K, 24K, 43K, 50K, 120K and 160K were detected. An additional polypeptide of 10K was detected by Western blot analysis. The two highest Mr species sometimes appeared as one band, of which only the 120K polypeptide was glycosylated. In the presence of tunicamycin gp120 was no longer detectable and a non-glycosylated precursor of 75K was found instead. Pulse-chase experiments suggested that the smaller polypeptides p24 and p15 are cleavage products of both p160 and p50. Western blot analysis using a rabbit serum directed against p26 of equine infectious anaemia virus (EIAV) and an anti-EIAV horse serum from a field case of infection revealed a cross-reactivity with p24 of FIV. Cat sera collected late after experimental FIV infection recognized p26 of EIAV, indicating a reciprocal cross-reactivity.
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Publication Date: 1990-03-01 PubMed ID: 1690264DOI: 10.1099/0022-1317-71-3-739Google Scholar: Lookup
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  • Comparative Study
  • Journal Article

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.

The study explores the overlapping antigenic characteristics between the Feline Immunodeficiency Virus (FIV) and the Equine Infectious Anaemia Virus (EIAV).

Research Methodology

  • The team cultivated the Feline Immunodeficiency Virus (FIV) in cat lymphocyte and thymocyte cultures. The virus was then labelled either with L-[35S]methionine or [3H]glucosamine.
  • Through immunoprecipitation, the research identified virus-produced proteins.
  • The study detected polypeptides with specific measured molecular weight (Mr) values, including 15K, 24K, 43K, 50K, 120K, and 160K. An additional 10K polypeptide was discovered through Western blot analysis.

Key Findings

  • The two highest Mr value species notably appeared as one band, wherein only the 120K polypeptide was glycosylated.
  • In the presence of a drug called tunicamycin, gp120 became undetectable, with a non-glycosylated precursor of 75K taking its place.
  • Experiments showed that smaller polypeptides, p24 and p15, are likely to be cleavage products of both p160 and p50.
  • Western blot analysis revealed that serum obtained from a rabbit directed against p26 of EIAV, as well as anti-EIAV horse serum from a field infection case, manifest cross-reactivity with p24 of FIV.
  • It was also observed that cat sera collected late after an experimental FIV infection recognized p26 of EIAV, thereby demonstrating a reciprocal cross-reactivity.

Significance and Implications

  • Identifying the structure and behaviour of FIV proteins, as well as possible *shared antigenic sites*, contributes to our comprehensive understanding of retrovirus biology and the potential for shared treatments or immunization strategies.
  • The observation of cross-reactivity between FIV and EIAV proteins suggests an antigenic similarity,
    which could potentially inform the development of diagnostic tools or treatments utilising shared immunological responses.

Cite This Article

APA
Egberink HF, Ederveen J, Montelaro RC, Pedersen NC, Horzinek MC, Koolen MJ. (1990). Intracellular proteins of feline immunodeficiency virus and their antigenic relationship with equine infectious anaemia virus proteins. J Gen Virol, 71 ( Pt 3), 739-743. https://doi.org/10.1099/0022-1317-71-3-739

Publication

The Journal of general virology
ISSN: 0022-1317
NlmUniqueID: 0077340
Country: England
Language: English
Volume: 71 ( Pt 3)
Pages: 739-743

Researcher Affiliations

Egberink, H F
  • Department of Virology, Veterinary Faculty, State University, Utrecht, The Netherlands.
Ederveen, J
    Montelaro, R C
      Pedersen, N C
        Horzinek, M C
          Koolen, M J

            MeSH Terms

            • Animals
            • Blotting, Western
            • Cats
            • Cell Transformation, Viral
            • Epitopes / analysis
            • Glucosamine / metabolism
            • Glycoproteins / biosynthesis
            • Glycoproteins / isolation & purification
            • Infectious Anemia Virus, Equine / analysis
            • Infectious Anemia Virus, Equine / immunology
            • Methionine / metabolism
            • Molecular Weight
            • Sulfur Radioisotopes
            • Tritium
            • Tunicamycin / pharmacology
            • Viral Proteins / analysis
            • Viral Proteins / biosynthesis
            • Viral Proteins / immunology
            • Visna-maedi virus / analysis
            • Visna-maedi virus / immunology
            • Visna-maedi virus / metabolism

            Citations

            This article has been cited 23 times.
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