Features of the Env leader protein and the N-terminal Gag domain of feline foamy virus important for virus morphogenesis

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• 作者：Geiselhart ; Verena ; Schwantes ; Astrid ; Bastone ; Patrizia ; Frech ; Matthias ; Lö ; chelt ; Martin
• 关键词：Foamy virus ; Env-Gag interaction
• 刊名：Virology
• 出版年：2003
• 出版时间：June 5, 2003
• 年：2003
• 卷：310
• 期：2
• 页码：235-244
• 全文大小：491 K

文摘

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.