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PRA1 co-localizes with envelope but does not influence primate lentivirus production, infectivity or envelope incorporation

Philippe Blancou

New England Regional Primate Research Center, Harvard Medical School, One Pine Hill Drive, Southborough, MA 01772-9102, USA

Correspondence
Ronald C. Desrosiers
ronald_desrosiers{at}hms.harvard.edu

The results of yeast and mammalian two-hybrid assays previously indicated complex formation between prenylated Rab acceptor 1 (PRA1) and the cytoplasmic domain of gp41 (gp41CD) for both the human and simian immunodeficiency viruses [Evans, D. T., Tilman, K. C. & Desrosiers, R. C. (2002). J Virol 76, 327–337]. The assembly and release of infectious virus particles was studied under conditions of PRA1 overexpression in a transient transfection assay or suppression by RNA interference. Although a clear pattern of co-localization of PRA1 and gp41 was observed, no changes in virion release, infectivity or envelope content were observed as a result of either PRA1 suppression or overexpression. These data show that PRA1 co-localizes with gp41 inside cells and they are consistent with a direct or indirect interaction between these proteins. However, variation in the levels of PRA1 expression did not influence virion production, infectivity or envelope incorporation under the conditions of these assays.

Present address: Unité d'immunologie-endocrinologie cellulaire et moléculaire, Ecole nationale vétérinaire de Nantes, BP 40706, 44307 Nantes Cedex 3, France.