PMID: 9445069Jan 28, 1998Paper

Mutational analysis of the fusion peptide of Moloney murine leukemia virus transmembrane protein p15E

Journal of Virology
N L ZhuW F Anderson

Abstract

Fusion peptides are hydrophobic sequences located at the N terminus of the transmembrane (TM) envelope proteins of the orthomyxoviruses and paramyxoviruses and several retroviruses. The Moloney murine leukemia virus TM envelope protein, p15E, contains a hydrophobic stretch of amino acids at its N terminus followed by a region rich in glycine and threonine residues. A series of single amino acid substitutions were introduced into this region, and the resulting proteins were examined for their abilities to be properly processed and transported to the cell surface and to induce syncytia in cells expressing the ecotropic receptor. One substitution in the hydrophobic core and several substitutions in the glycine/threonine-rich region that prevented both cell-cell fusion and the transduction of NIH 3T3 cells when incorporated into retroviral vector particles were identified. In addition, one mutation that enhanced the fusogenicity of the resulting envelope protein was identified. The fusion-defective mutants trans dominantly interfered with the ability of the wild-type envelope protein to cause syncytium formation in a cell-cell fusion assay, although no trans-dominant inhibition of transduction was observed. Certain substitutions in...Continue Reading

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Citations

Jan 29, 2003·Journal of Virology·Wendy MaurySarahann Bradley
Jul 7, 2001·Human Gene Therapy·E M GordonF L Hall
Jul 20, 2007·Journal of Virology·Samuel L Murphy, Glen N Gaulton
Apr 29, 2004·Journal of Virology·Andrey A Kolokoltsov, Robert A Davey
Jun 17, 1998·Journal of Virology·B Weimin WuW F Anderson
Jun 17, 1998·Journal of Virology·Y ZhaoP M Cannon
Jan 22, 2008·Experimental and Molecular Pathology·Raquel F EpandYanina Rozenberg-Adler

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