The preparation and biochemical characterization of intact capsids of equine infectious anemia virus.
Abstract: Capsids of equine infectious anemia virus have been isolated as cone-shaped particles 60 x 120 nm in size. Detergent treatment of whole virus followed by two cycles of rate-zonal centrifugation in Ficoll produces these capsids in a yield of approximately 10%. The major protein components are the gag-encoded p11 nucleocapsid protein and p26 capsid protein, which are present in equimolar amounts. Substantial cleavage of p11 to p6 and p4 can be observed under conditions where the viral protease packaged in the capsid is enzymatically active.
Publication Date: 1989-04-28 PubMed ID: 2541703DOI: 10.1016/0006-291x(89)92459-5Google Scholar: Lookup
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- Journal Article
- Research Support
- U.S. Gov't
- P.H.S.
Summary
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This research investigates the extraction and biochemical properties of a virus that infects horses, equine infectious anemia virus. The researchers managed to isolate the virus capsids, and found that the main protein components are p11 nucleocapsid protein and p26 capsid protein.
Methodology and Findings
- The team carried out studies on equine infectious anemia virus (EIAV), a virus related to the human immunodeficiency virus (HIV) that affects horses.
- The virus was treated with a detergent, followed by two levels of rate-zonal centrifugation in Ficoll, a type of sugar. This process allowed the capsids (protein shell of a virus) to be isolated.
- The isolated capsids were found to be cone-shaped particles of 60 x 120 nm in size. The yield of these isolated capsids from this process was about 10% of the whole virus.
Main Protein Components
- The main protein components of these capsids were the gag-encoded p11 nucleocapsid protein and p26 capsid protein.
- Both of these proteins were found to be present in equal amounts.
- The researchers also found that under certain conditions, a significant portion of p11 was cleaved (or cut) into p6 and p4. This appeared to happen when the viral protease (an enzyme that breaks down proteins) was active within the capsid.
Significance of the Study
- The findings of this study could further our understanding of how EIAV functions at a biochemical level.
- This could potentially lead to new ways of combatting the virus, which has significant implications for equine health.
- Given the similarities between EIAV and HIV, this study might also contribute to broader research into retroviruses and potentially aid in the development of therapies for human diseases.
Cite This Article
APA
Roberts MM, Oroszlan S.
(1989).
The preparation and biochemical characterization of intact capsids of equine infectious anemia virus.
Biochem Biophys Res Commun, 160(2), 486-494.
https://doi.org/10.1016/0006-291x(89)92459-5 Publication
Researcher Affiliations
- Laboratory of Molecular Virology and Carcinogenesis, NCI-Frederick Cancer Research Facility, Maryland 21701.
MeSH Terms
- Capsid / enzymology
- Capsid / isolation & purification
- Capsid / ultrastructure
- Centrifugation, Zonal
- Detergents
- Electrophoresis, Polyacrylamide Gel
- Hydrogen-Ion Concentration
- Infectious Anemia Virus, Equine / analysis
- Infectious Anemia Virus, Equine / enzymology
- Infectious Anemia Virus, Equine / ultrastructure
- RNA, Viral / isolation & purification
- Viral Core Proteins / isolation & purification
- Viral Core Proteins / ultrastructure
Grant Funding
- N01-CO-74101 / NCI NIH HHS
Citations
This article has been cited 23 times.- Mótyán JA, Miczi M, Oroszlan S, Tőzsér J. Specificity of the HIV-1 Protease on Substrates Representing the Cleavage Site in the Proximal Zinc-Finger of HIV-1 Nucleocapsid Protein. Viruses 2021 Jun 8;13(6).
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- Chen K, Tjandra N. Determining interdomain structure and dynamics of a retroviral capsid protein in the presence of oligomerization: implication for structural transition in capsid assembly. Biochemistry 2013 Aug 13;52(32):5365-71.
- Chen K, Piszczek G, Carter C, Tjandra N. The maturational refolding of the β-hairpin motif of equine infectious anemia virus capsid protein extends its helix α1 at capsid assembly locus. J Biol Chem 2013 Jan 18;288(3):1511-20.
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