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Journal of Virology, December 2007, p. 13631-13639, Vol. 81, No. 24
0022-538X/07/$08.00+0     doi:10.1128/JVI.01688-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Ubiquitin Depletion and Dominant-Negative VPS4 Inhibit Rhabdovirus Budding without Affecting Alphavirus Budding{triangledown}

Gwen M. Taylor,1 Phyllis I. Hanson,2 and Margaret Kielian1*

Department of Cell Biology, Albert Einstein College of Medicine, Bronx, New York 10461,1 Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 631102

Received 3 August 2007/ Accepted 21 September 2007

The budding reactions of a number of enveloped viruses use the cellular machinery involved in the formation of the luminal vesicles of endosomal multivesicular bodies (MVB). Budding of these viruses is dependent on the presence of specific late-domain motifs in membrane-associated viral proteins. Such budding reactions usually involve ubiquitin and are blocked by expression of an ATPase-deficient form of VPS4, a cellular AAA+ ATPase believed to be required late in the MVB pathway for the disassembly/release of the MVB machinery. Here we examined the role of the MVB pathway in the budding of the late-domain-containing rhabdovirus vesicular stomatitis virus (VSV) and the alphavirus Semliki Forest virus (SFV). We tested early and late steps in the MVB pathway by depleting ubiquitin with the proteasome inhibitor MG-132 and by using cell lines inducibly expressing VPS4A or VPS4B protein. As previously shown, VSV budding was strongly dependent on ubiquitin. In contrast to the findings of previous studies with VPS4A, expression of ATPase-deficient mutants of either VPS4A or VPS4B inhibited VSV budding. Inhibition by VPS4 required the presence of the PPPY late domain on the VSV matrix protein and resulted in the accumulation of nonreleased VSV particles at the plasma membrane. In contrast, SFV budding was independent of both ubiquitin and the activity of VPS4, perhaps reflecting the important role of the highly organized envelope protein lattice during alphavirus budding.

* Corresponding author. Mailing address: Department of Cell Biology, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461. Phone: (718) 430-3638. Fax: (718) 430-8574. E-mail: kielian{at}aecom.yu.edu

{triangledown} Published ahead of print on 3 October 2007.

Journal of Virology, December 2007, p. 13631-13639, Vol. 81, No. 24
0022-538X/07/$08.00+0     doi:10.1128/JVI.01688-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



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