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J. Biol. Chem., Vol. 281, Issue 42, 31778-31789, October 20, 2006

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The p14 Fusion-associated Small Transmembrane (FAST) Protein Effects Membrane Fusion from a Subset of Membrane Microdomains^*

Jennifer A. Corcoran, Jayme Salsman¹, Roberto de Antueno, Ahmed Touhami, Manfred H. Jericho, Eileen K. Clancy², and Roy Duncan³

From the Departments of Microbiology and Immunology and Physics, Dalhousie University, Halifax, Nova Scotia B3H 1X5, Canada

The reovirus fusion-associated small transmembrane (FAST) proteins are a unique family of viral membrane fusion proteins. These nonstructural viral proteins induce efficient cell-cell rather than virus-cell membrane fusion. We analyzed the lipid environment in which the reptilian reovirus p14 FAST protein resides to determine the influence of the cell membrane on the fusion activity of the FAST proteins. Topographical mapping of the surface of fusogenic p14-containing liposomes by atomic force microscopy under aqueous conditions revealed that p14 resides almost exclusively in thickened membrane microdomains. In transfected cells, p14 was found in both Lubrol WX- and Triton X-100-resistant membrane complexes. Cholesterol depletion of donor cell membranes led to preferential disruption of p14 association with Lubrol WX (but not Triton X-100)-resistant membranes and decreased cell-cell fusion activity, both of which were reversed upon subsequent cholesterol repletion. Furthermore, co-patching analysis by fluorescence microscopy indicated that p14 did not co-localize with classical lipidanchored raft markers. These data suggest that the p14 FAST protein associates with heterogeneous membrane microdomains, a distinct subset of which is defined by cholesterol-dependent Lubrol WX resistance and which may be more relevant to the membrane fusion process.

Received for publication, March 20, 2006 , and in revised form, August 24, 2006.

^* This work was supported in part by grants from the Canadian Institutes of Health Research (to R. D.) and by grants from the Natural Sciences and Engineering Research Council (to M. H. J.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains detailed experimental results and methods for Fig. 1C.

¹ Supported by scholarships from the Natural Sciences and Engineering Research Council, the Cancer Research Training Program of Cancer Care Nova Scotia, and the Nova Scotia Health Research Foundation.

² Supported by a scholarship from the Cancer Research Training Program of Cancer Care Nova Scotia.

³ Recipient of a Regional Partnerships Program Investigator Award from the Canadian Institutes of Health Research. To whom correspondence should be addressed: Dept. of Microbiology and Immunology, Tupper Medical Bldg., Rm. 7S, Dalhousie University, Halifax, Nova Scotia B3H 1X5, Canada. Tel.: 902-494-6770; Fax: 902-494-5125; E-mail: roy.duncan{at}dal.ca.

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This article has been cited by other articles:

				E. K. Clancy and R. Duncan Reovirus FAST Protein Transmembrane Domains Function in a Modular, Primary Sequence-Independent Manner To Mediate Cell-Cell Membrane Fusion J. Virol., April 1, 2009; 83(7): 2941 - 2950. [Abstract] [Full Text] [PDF]