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Home / Equine Research Bank / J Virol / Enhanced sensitivity to neutralizing antibodies in a variant...
Journal of virology1995; 69(3); 1493-1499; doi: 10.1128/JVI.69.3.1493-1499.1995

Enhanced sensitivity to neutralizing antibodies in a variant of equine infectious anemia virus is linked to amino acid substitutions in the surface unit envelope glycoprotein.

Abstract: Serial passage of the prototype (PR) cell-adapted Wyoming strain of equine infectious anemia virus (EIAV) in fetal donkey dermal (FDD) rather than fetal horse (designated fetal equine kidney [FEK]) cell cultures resulted in the generation of a variant virus strain which produced accelerated cytopathic effects in FDD cells and was 100- to 1,000-fold more sensitive to neutralizing antibodies than its parent. This neutralization-sensitive variant was designated the FDD strain. Although there were differences in glycosylation between the PR and FDD strains, passage of the FDD virus in FEK cells did not reduce its sensitivity to neutralizing antibody. Nucleotide sequencing of the region encoding the surface unit (SU) protein from the FDD strain revealed nine amino acid substitutions compared with the PR strain. Two of these substitutions resulted in changes in the polarity of charge, four caused the introduction of a charged residue, and three had no net change in charge. Nucleotide sequence analysis was extended to the region of the FDD virus genome encoding the extracellular domain of the transmembrane envelope glycoprotein (TM). Unlike the situation with the FDD virus coding region, there were minor variations in nucleotide sequence between individual molecular clones containing this region of the TM gene. Although each clone contained three nucleotide substitutions compared with the PR strain, only one of these was common to all, and this did not affect the amino acid content. Of the remaining two nucleotide substitutions, only one resulted in an amino acid change, and in each case, this change appeared to be conservative. To determine if amino acid substitutions in the SU protein of FDD cell-grown viruses were responsible for the enhanced sensitivity to neutralizing antibodies, chimeric viruses were constructed by using an infectious molecular clone of EIAV. These chimeric viruses contained all of the amino acid substitutions found in the FDD virus strain and were significantly more sensitive to neutralizing antibodies than viruses from the parental (PR) molecular clone. These results demonstrated that sensitivity to neutralizing antibodies in EIAV can be conferred by amino acid residues in the SU protein. However, such amino acid substitutions were not sufficient to enhance cytopathogenicity, as the chimeric viruses did not cause excessive degenererative effects in FDD cells, as was observed with the parental FDD virus strain.
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Publication Date: 1995-03-01 PubMed ID: 7853482PubMed Central: PMC188739DOI: 10.1128/JVI.69.3.1493-1499.1995Google 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 research investigates a variant of the equine infectious anemia virus (EIAV) that’s more sensitive to neutralizing antibodies due to alterations in amino acids in the glycoprotein on the virus’s surface. The study’s findings indicate that these amino acid changes can increase the virus’s vulnerability to neutralizing antibodies, but don’t necessarily increase the virus’s destructive impact on cells.

Study Background and Methodology

  • The research focused on a variant of equine infectious anemia virus (EIAV), a disease affecting horses, which presented enhanced sensitivity to neutralizing antibodies, proteins that directly counteract the effects of viruses.
  • The viral variant was created through serial passage (repeated transmission) of the virus in fetal donkey dermal (FDD) cells instead of fetal horse kidney (FEK) cells, giving rise to a strain termed FDD.
  • The FDD strain, while inducing faster cell damage in FDD cells, showed all the way from 100 to 1,000-fold increased sensitivity to neutralizing antibodies compared to the original PR strain.

Results of the Research

  • Nucleotide sequencing of the region encoding the surface unit (SU) protein from the FDD strain revealed nine amino acid substitutions compared to the PR strain. Some of these substitutions affected the electrical charge (polarity) and others introduced a charged residue while some did not affect the overall charge.
  • The research also included detailed analysis of the sequence differences in the transmembrane envelope glycoprotein (TM) domain, but this revealed only minor variations between individual molecular clones.
  • To confirm whether these amino acid substitutions in the SU protein were causing enhanced neutralizing antibody sensitivity, researchers created chimeric (hybrid) viruses. These viruses contained all the amino acid alterations identified in the FDD strain and demonstrated significantly greater sensitivity to neutralizing antibodies than the parent PR strain.

Significance and Conclusion

  • The study provides evidence that alterations in specific amino acids in the SU protein can significantly increase a virus’s susceptibility to neutralizing antibodies. This shows how the virus’s genetic makeup can determine its vulnerability to the immune system’s defenses.
  • However, while these amino acid changes can significantly enhance antibody susceptibility, they don’t necessarily make the virus more harmful or destructive to cells. This suggests that additional factors besides amino acid substitutions must be responsible for the virus’s ability to cause cell damage.

Cite This Article

APA
Cook RF, Berger SL, Rushlow KE, McManus JM, Cook SJ, Harrold S, Raabe ML, Montelaro RC, Issel CJ. (1995). Enhanced sensitivity to neutralizing antibodies in a variant of equine infectious anemia virus is linked to amino acid substitutions in the surface unit envelope glycoprotein. J Virol, 69(3), 1493-1499. https://doi.org/10.1128/JVI.69.3.1493-1499.1995

Publication

Journal of virology
ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 69
Issue: 3
Pages: 1493-1499

Researcher Affiliations

Cook, R F
  • Department of Veterinary Science, Gluck Equine Research Center, University of Kentucky, Lexington 40546.
Berger, S L
    Rushlow, K E
      McManus, J M
        Cook, S J
          Harrold, S
            Raabe, M L
              Montelaro, R C
                Issel, C J

                  MeSH Terms

                  • Amino Acid Sequence
                  • Antibodies, Viral / immunology
                  • Antigens, Viral / immunology
                  • Base Sequence
                  • Genes, Viral
                  • Glycoproteins / chemistry
                  • Glycoproteins / immunology
                  • Infectious Anemia Virus, Equine / genetics
                  • Infectious Anemia Virus, Equine / immunology
                  • Molecular Sequence Data
                  • Mutation
                  • Neutralization Tests
                  • Viral Envelope Proteins / chemistry
                  • Viral Envelope Proteins / genetics
                  • Viral Envelope Proteins / immunology
                  • Viral Fusion Proteins / chemistry
                  • Viral Fusion Proteins / immunology
                  • Viral Structural Proteins / genetics

                  Grant Funding

                  • 1-T32-AI-07487-01 / NIAID NIH HHS
                  • R01AI25850 / NIAID NIH HHS

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