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Home / Equine Research Bank / J Virol / Equine infectious anemia virus Gag polyprotein late domain s...
Journal of virology1998; 72(12); 10218-10221; doi: 10.1128/JVI.72.12.10218-10221.1998

Equine infectious anemia virus Gag polyprotein late domain specifically recruits cellular AP-2 adapter protein complexes during virion assembly.

Abstract: We have identified an interaction between the equine infectious anemia virus (EIAV) late assembly domain and the cellular AP-2 clathrin-associated adapter protein complex. A YXXL motif within the EIAV Gag late assembly domain was previously characterized as a sequence critical for release of assembling virions. We now show that this YXXL sequence interacts in vitro with the AP-50 subunit of the AP-2 complex, while the functionally interchangeable late assembly domains carried by the Rous sarcoma virus p2b protein and human immunodeficiency virus type 1 p6 protein, which utilize PPPY and PTAPP L domains, respectively, do not bind AP-50 in vitro. In addition, EIAV late domain mutants containing mutations that have previously been shown to abrogate budding also exhibit marked decreases in AP-50 binding efficiencies. A role for AP-2 complex in viral assembly is supported by immunofluorescence analysis of EIAV-infected equine dermal cells demonstrating specific colocalization of the alpha adaptin subunit of AP-2 with the EIAV p9 protein at sites of virus budding on the plasma membrane. These data provide strong evidence that EIAV utilizes the cellular AP-2 complex to accomplish virion assembly and release.
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Publication Date: 1998-11-13 PubMed ID: 9811764PubMed Central: PMC110572DOI: 10.1128/JVI.72.12.10218-10221.1998Google Scholar: Lookup
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  • 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) specifically interacts with cellular AP-2 adapter protein complexes during virion assembly.

Interactions Between EIAV and AP-2

  • The paper uncovers how the equine infectious anemia virus (EIAV) recruits cellular AP-2 adapter protein complexes as a part of it’s virion assembly process. The researchers have particularly highlighted the role of a YXXL motif in the EIAV Gag late assembly domain.
  • The YXXL sequence in the EIAV Gag late assembly domain is found to interact with the AP-50 subunit of the AP-2 complex. This finding denotes the critical role of the YXXL motif in the release of assembling virions.

Comparison with Other Viruses

  • When compared with the assembly domains of the Rous sarcoma virus p2b protein and human immunodeficiency virus type 1 p6 protein, the YXXL sequence is proven to be unique as the PPPY and PTAPP L domains of the other viruses do not bind with AP-50 in vitro.

Mutants and AP-50 Binding Efficiencies

  • EIAV late domain mutants with mutations that previously impeded budding were shown to have significantly lower AP-50 binding capacities. This shows that the mutations effect not only budding but also affect the interaction with cellular structures.

AP-2 Complex Role in Viral Assembly

  • The role of the AP-2 complex in viral assembly is reinforced through immunofluorescence analysis of EIAV-infected equine dermal cells. The results show specific colocalization of the alpha adaptin subunit of AP-2 with the EIAV p9 protein at the sites of virus budding on the plasma membrane.
  • These findings provide compelling evidence that the EIAV relies on the cellular AP-2 complex in order to complete virion assembly and initiate release.

Cite This Article

APA
Puffer BA, Watkins SC, Montelaro RC. (1998). Equine infectious anemia virus Gag polyprotein late domain specifically recruits cellular AP-2 adapter protein complexes during virion assembly. J Virol, 72(12), 10218-10221. https://doi.org/10.1128/JVI.72.12.10218-10221.1998

Publication

Journal of virology
ISSN: 0022-538X
NlmUniqueID: 0113724
Country: United States
Language: English
Volume: 72
Issue: 12
Pages: 10218-10221

Researcher Affiliations

Puffer, B A
  • Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, USA.
Watkins, S C
    Montelaro, R C

      MeSH Terms

      • Amino Acid Sequence
      • Animals
      • COS Cells
      • DNA-Binding Proteins / chemistry
      • DNA-Binding Proteins / physiology
      • Gene Products, gag / chemistry
      • Gene Products, gag / genetics
      • Gene Products, gag / physiology
      • Humans
      • Infectious Anemia Virus, Equine / genetics
      • Infectious Anemia Virus, Equine / growth & development
      • Infectious Anemia Virus, Equine / physiology
      • Macromolecular Substances
      • Mutagenesis, Site-Directed
      • Protein Conformation
      • Recombinant Fusion Proteins / chemistry
      • Recombinant Fusion Proteins / genetics
      • Recombinant Fusion Proteins / physiology
      • Transcription Factor AP-2
      • Transcription Factors / chemistry
      • Transcription Factors / physiology

      Grant Funding

      • R01 CA049296 / NCI NIH HHS
      • 5R01CA49296 / NCI NIH HHS

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