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Journal of Virology, December 1998, p. 10218-10221, Vol. 72, No. 12
Department of Molecular Genetics and
Biochemistry1 and
Department of Cell
Biology and Physiology,2 University of
Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261
Received 16 June 1998/Accepted 21 August 1998
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
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.
Equine Infectious Anemia Virus Gag Polyprotein Late
Domain Specifically Recruits Cellular AP-2 Adapter Protein
Complexes during Virion Assembly
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.
*
Corresponding author. Mailing address: Department of
Molecular Genetics and Biochemistry, University of Pittsburgh School of
Medicine, W1144 Biomedical Science Tower, Pittsburgh, PA 15261. Phone:
(412) 648-8869. Fax: (412) 383-8859. E-mail:
rmont{at}pop.pitt.edu.
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