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Journal of Virology, October 2006, p. 9465-9480, Vol. 80, No. 19
0022-538X/06/$08.00+0     doi:10.1128/JVI.01049-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Human ESCRT-II Complex and Its Role in Human Immunodeficiency Virus Type 1 Release{dagger}

Charles Langelier,1 Uta K. von Schwedler,1 Robert D. Fisher,1 Ivana De Domenico,2 Paul L. White,1 Christopher P. Hill,1 Jerry Kaplan,2 Diane Ward,2 and Wesley I. Sundquist1*

Departments of Biochemistry,1 Pathology, University of Utah, Salt Lake City, Utah 841122

Received 22 May 2006/ Accepted 8 July 2006

The budding of many enveloped RNA viruses, including human immunodeficiency virus type 1 (HIV-1), requires some of the same cellular machinery as vesicle formation at the multivesicular body (MVB). In Saccharomyces cerevisiae, the ESCRT-II complex performs a central role in MVB protein sorting and vesicle formation, as it is recruited by the upstream ESCRT-I complex and nucleates assembly of the downstream ESCRT-III complex. Here, we report that the three subunits of human ESCRT-II, EAP20, EAP30, and EAP45, have a number of properties in common with their yeast orthologs. Specifically, EAP45 bound ubiquitin via its N-terminal GRAM-like ubiquitin-binding in EAP45 (GLUE) domain, both EAP45 and EAP30 bound the C-terminal domain of TSG101/ESCRT-I, and EAP20 bound the N-terminal half of CHMP6/ESCRT-III. Consistent with its expected role in MVB vesicle formation, (i) human ESCRT-II localized to endosomal membranes in a VPS4-dependent fashion and (ii) depletion of EAP20/ESCRT-II and CHMP6/ESCRT-III inhibited lysosomal targeting and downregulation of the epidermal growth factor receptor, albeit to a lesser extent than depletion of TSG101/ESCRT-I. Nevertheless, HIV-1 release and infectivity were not reduced by efficient small interfering RNA depletion of EAP20/ESCRT-II or CHMP6/ESCRT-III. These observations indicate that there are probably multiple pathways for protein sorting/MVB vesicle formation in human cells and that HIV-1 does not utilize an ESCRT-II-dependent pathway to leave the cell.

* Corresponding author. Mailing address: Department of Biochemistry, 15 N. Medical Drive East, Room 4100, University of Utah School of Medicine, Salt Lake City, UT 84112-5650. Phone: (801) 585-5402. Fax: (801) 581-7959. E-mail: wes{at}biochem.utah.edu.

{dagger} Supplemental material for this article may be found at http://jvi.asm.org.

Journal of Virology, October 2006, p. 9465-9480, Vol. 80, No. 19
0022-538X/06/$08.00+0     doi:10.1128/JVI.01049-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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