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  • Title: Features of the Env leader protein and the N-terminal Gag domain of feline foamy virus important for virus morphogenesis.
    Author: Geiselhart V, Schwantes A, Bastone P, Frech M, Löchelt M.
    Journal: Virology; 2003 Jun 05; 310(2):235-44. PubMed ID: 12781711.
    Abstract:
    Previous studies have shown that foamy virus (FV) particle budding, especially the involvement of the viral env glycoprotein is different from that of other (ortho) retroviruses: the N-terminal Env leader protein Elp is a constituent of released FV particles. A defined sequence in Elp required for particle budding binds to the MA domain of Gag. To extend these findings, we show that feline FV Elp is a membrane-anchored protein with the N-terminus located inside the particle. Thus, the internal/cytoplasmic domain of Elp has the correct topology for interacting with Gag during budding. In addition to Elp, an Elp-related protein of about 9 kDa was shown to be virion associated and is probably generated by cellular signal peptidases. Besides the function of Elp binding, the N-terminal domain of Gag was shown to be required for proper localization of feline FV Gag to the cytoplasm and the perinuclear/nuclear region.
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