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Home / Equine Research Bank / J Virol / Equine infectious anemia virus utilizes a YXXL motif within ...
Journal of virology1997; 71(9); 6541-6546; doi: 10.1128/JVI.71.9.6541-6546.1997

Equine infectious anemia virus utilizes a YXXL motif within the late assembly domain of the Gag p9 protein.

Abstract: We have previously demonstrated that the Gag p9 protein of equine infectious anemia virus (EIAV) is functionally homologous with Rous sarcoma virus (RSV) p2b and human immunodeficiency virus type 1 (HIV-1) p6 in providing a critical late assembly function in RSV Gag-mediated budding from transfected COS-1 cells (L. J. Parent et al., J. Virol. 69:5455-5460, 1995). In light of the absence of amino acid sequence homology between EIAV p9 and the functional homologs of RSV and HIV-1, we have now designed an EIAV Gag-mediated budding assay to define the late assembly (L) domain peptide sequences contained in the EIAV p9 protein. The results of these particle budding assays revealed that expression of EIAV Gag polyprotein in COS-1 cells yielded extracellular Gag particles with a characteristic density of 1.18 g/ml, while expression of EIAV Gag polyprotein lacking p9 resulted in a severe reduction in the release of extracellular Gag particles. The defect in EIAV Gag polyprotein particle assembly could be corrected by substituting either the RSV p2b or HIV-1 p6 protein for EIAV p9. These observations demonstrated that the L domains of EIAV, HIV-1, and RSV were interchangeable in mediating assembly of EIAV Gag particles in the COS-1 cell budding assay. To localize the L domain of EIAV p9, we next assayed the effects of deletions and site-specific mutations in the p9 protein on its ability to mediate budding of EIAV Gag particles. Analyses of EIAV Gag constructs with progressive N-terminal or C-terminal deletions of the p9 protein identified a minimum sequence of 11 amino acids (Q20N21L22Y23P24D25L26S27E28I29K30) capable of providing the late assembly function. Alanine scanning studies of this L-domain sequence demonstrated that mutations of residues Y23, P24, and L26 abrogated the p9 late budding function; mutations of other residues in the p9 L domain did not substantially affect the level of EIAV Gag particle assembly. These data indicate that the L domain in EIAV p9 utilizes a YXXL motif which we hypothesize may interact with cellular proteins to facilitate virus particle budding from infected cells.
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Publication Date: 1997-09-01 PubMed ID: 9261374PubMed Central: PMC191930DOI: 10.1128/JVI.71.9.6541-6546.1997Google Scholar: Lookup
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  • Non-U.S. Gov't
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  • U.S. Gov't
  • P.H.S.

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 explores how the equine infectious anemia virus (EIAV) uses a specific sequence within the Gag p9 protein to facilitate viral particle assembly. This paper identifies the critical sequence of amino acids in the late assembly domain and shows that small alterations can disrupt viral budding.

Objective and Methodology

  • The research aims to identify the essential peptide sequences within the EIAV p9 protein that are responsible for late viral assembly.
  • The researchers designed an EIAV Gag (a group-specific antigen part of the complex retrovirus structure) mediated budding assay, a type of experiment used to measure the formation and release of viral particles.
  • The assay was used on transfected COS-1 cells to compare the assembly process between EIAV, RSV, and HIV-1 viruses.

Findings

  • The study found that the EIAV Gag polyprotein expressions created extracellular Gag particles, while an absence of p9 protein led to a significant reduction in the release of such particles.
  • Interestingly, the researchers noted that substituting either the RSV p2b or HIV-1 p6 protein for EIAV p9 could correct this assembly defect. This suggests that these proteins’ late assembly domains are interchangeable.
  • The research used progressive N-terminal or C-terminal deletions of the p9 protein and site-specific mutations to identify an 11 amino acid sequence responsible for providing the late assembly function.
  • Substituting three specific residues within this sequence (Y23, P24, L26) with alanine disrupted the late budding function. This suggests that these residues are essential for the assembly of the EIAV Gag particles.

Conclusion

  • Based on the obtained results, the researchers concluded that the EIAV p9 protein uses a YXXL motif within its late assembly domain to facilitate viral particle assembly and release.
  • Specific interplay with cellular proteins is hypothesized to be facilitated by this motif, indicating a potential target for interventions to disrupt the virus’s lifecycle.

Cite This Article

APA
Puffer BA, Parent LJ, Wills JW, Montelaro RC. (1997). Equine infectious anemia virus utilizes a YXXL motif within the late assembly domain of the Gag p9 protein. J Virol, 71(9), 6541-6546. https://doi.org/10.1128/JVI.71.9.6541-6546.1997

Publication

Journal of virology
ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 71
Issue: 9
Pages: 6541-6546

Researcher Affiliations

Puffer, B A
  • Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pennsylvania 15261, USA.
Parent, L J
    Wills, J W
      Montelaro, R C

        MeSH Terms

        • Amino Acid Sequence
        • Animals
        • Binding Sites
        • COS Cells
        • Gene Products, gag / chemistry
        • Gene Products, gag / physiology
        • Infectious Anemia Virus, Equine / physiology
        • Molecular Sequence Data
        • Virus Assembly

        Grant Funding

        • 5R01CA49296 / NCI NIH HHS
        • K11A101148 / PHS HHS
        • R01CA47482 / NCI NIH HHS

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