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Journal of Virology, August 2003, p. 8440-8447, Vol. 77, No. 15
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.15.8440-8447.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Equine Infectious Anemia Virus Utilizes Host Vesicular Protein Sorting Machinery during Particle Release

Giancarlo O. Tanzi,1,2 Andrew J. Piefer,1 and Paul Bates1,2*

Department of Microbiology,1 Graduate Program in Cell and Molecular Biology, University of Pennsylvania School of Medicine, Philadelphia, Pennsylvania 19104-60762

Received 23 January 2003/ Accepted 9 May 2003

A final step in retrovirus assembly, particle release from the cell, is modulated by a small motif in the Gag protein known as a late domain. Recently, human immunodeficiency virus type 1 (HIV-1) and Moloney murine leukemia virus (M-MuLV) were shown to require components of the cellular vacuolar protein sorting (VPS) machinery for efficient viral release. HIV-1 interacts with the VPS pathway via an association of HIV-1 Gag with TSG101, a component of the cellular complexes involved in VPS. Equine infectious anemia virus (EIAV) is unique among enveloped viruses studied to date because it utilizes a novel motif, YPDL in Gag, as a late domain. Our analysis of EIAV assembly demonstrates that EIAV Gag release is blocked by inhibition of the VPS pathway. However, in contrast to HIV-1, EIAV Gag release is insensitive to TSG101 depletion and EIAV particles do not contain significant levels of TSG101. Finally, we demonstrate that fusing EIAV Gag directly with another cellular component of the VPS machinery, VPS28, can restore efficient release of an EIAV Gag late-domain mutant. These results provide evidence that retroviruses can interact with the cellular VPS machinery in several different ways to accomplish particle release.

* Corresponding author. Mailing address: Department of Microbiology, University of Pennsylvania School of Medicine, 225 Johnson Pavilion, 3610 Hamilton Walk, Philadelphia, PA 19104-6076. Phone: (215) 573-3509. Fax: (215) 573-9068. E-mail: pbates{at}mail.med.upenn.edu.

Journal of Virology, August 2003, p. 8440-8447, Vol. 77, No. 15
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.15.8440-8447.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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