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Home / Equine Research Bank / J Virol / Structure of equine infectious anemia virus matrix protein.
Journal of virology2002; 76(4); 1876-1883; doi: 10.1128/jvi.76.4.1876-1883.2002

Structure of equine infectious anemia virus matrix protein.

Abstract: The Gag polyprotein is key to the budding of retroviruses from host cells and is cleaved upon virion maturation, the N-terminal membrane-binding domain forming the matrix protein (MA). The 2.8-A resolution crystal structure of MA of equine infectious anemia virus (EIAV), a lentivirus, reveals that, despite showing no sequence similarity, more than half of the molecule can be superimposed on the MAs of human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV). However, unlike the structures formed by HIV-1 and SIV MAs, the oligomerization state observed is not trimeric. We discuss the potential of this molecule for membrane binding in the light of conformational differences between EIAV MA and HIV or SIV MA.
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Publication Date: 2002-01-19 PubMed ID: 11799182PubMed Central: PMC135893DOI: 10.1128/jvi.76.4.1876-1883.2002Google 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.

The research article comprises a study about the structure of the matrix protein (MA) of equine infectious anemia virus (EIAV), comparing it to the MAs of HIV-1 and SIV and discussing its potential for membrane binding.

Overview of the Research

  • The article focuses on understanding the matrix protein of EIAV. The matrix protein plays a crucial role in retroviruses, as it’s formed from the cleavage of the Gag polyprotein, aiding in the release of retroviruses from host cells.
  • The structure of this MA from EIAV was examined at a resolution of 2.8 Angstroms using crystallography, providing a detailed visualization of the molecular arrangement.

Comparison with other Matrix Proteins

  • A key aspect of the research was to compare the EIAV MA structure with MAs from other retroviruses, specifically human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV).
  • Despite showing no sequence similarity, more than half of the EIAV MA could be superimposed on the MAs of HIV-1 and SIV, indicating similar structural patterns.
  • However, the research noted a difference in that the oligomerization state of EIAV MA is not trimeric, unlike the structures formed by HIV-1 and SIV MAs.

Potential for Membrane Binding

  • The research discusses the potential of EIAV MA for binding to cellular membranes, a crucial step in the lifecycle of a retrovirus.
  • This discussion is informed by the observed conformational differences between the MAs of EIAV and those of HIV or SIV.
  • The differences suggest possible variations in membrane-binding capacity, which can provide insights into the unique characteristics of EIAV and its interaction with host cells.

Significance of the Research

  • Overall, the research provides insightful views into the structure of EIAV’s MA and how it compares to other well-studied retroviruses.
  • These findings can help in understanding the molecular mechanisms behind retroviral replication and budding as well as pave way for the development of potential antiretroviral therapies.

Cite This Article

APA
Hatanaka H, Iourin O, Rao Z, Fry E, Kingsman A, Stuart DI. (2002). Structure of equine infectious anemia virus matrix protein. J Virol, 76(4), 1876-1883. https://doi.org/10.1128/jvi.76.4.1876-1883.2002

Publication

Journal of virology
ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 76
Issue: 4
Pages: 1876-1883

Researcher Affiliations

Hatanaka, Hideki
  • Division of Structural Biology, Wellcome Trust Centre for Human Genetics, University of Oxford, Oxford OX3 7BN, United Kingdom.
Iourin, Oleg
    Rao, Zihe
      Fry, Elizabeth
        Kingsman, Alan
          Stuart, David I

            MeSH Terms

            • Amino Acid Sequence
            • Crystallization
            • Crystallography, X-Ray
            • Gene Products, gag / genetics
            • HIV Antigens / genetics
            • Infectious Anemia Virus, Equine / chemistry
            • Infectious Anemia Virus, Equine / metabolism
            • Models, Molecular
            • Molecular Sequence Data
            • Protein Conformation
            • Sequence Alignment
            • Simian Immunodeficiency Virus / metabolism
            • Viral Matrix Proteins / chemistry
            • Viral Matrix Proteins / genetics
            • Viral Proteins
            • gag Gene Products, Human Immunodeficiency Virus

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            Citations

            This article has been cited 21 times.
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