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C-Terminal truncations of syncytin-1 (ERVWE1 envelope) that increase its fusogenicity by Sascha Drewlo; Simone Leyting; Maria Kokozidou; François Mallet; Andy J.G. Pötgens is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is C-Terminal truncations of syncytin-1 (ERVWE1 envelope) that increase its fusogenicity about?

Syncytin-1, the envelope protein of ERVWE1, an endogenous retrovirus of the HERV-W family, plays an important role in regulating fusion of the placental trophoblast. At least one of its receptors is expressed on a variety of human cell types. Its ability to fuse cells makes it an attractive candidate molecule in gene therapy against cancer. We studied the relevance of sequences in the cytoplasmic tail of syncytin-1 for inducing cell-cell fusion. We generated a series of C-terminally truncated syncytin-1 variants. Sequences immediately adjacent to the transmembrane region of syncytin-1 were necessary for inducing optimal fusion, whereas the extreme C-terminus of syncytin-1 partially inhibited its fusogenicity. Two variants of syncytin-1, truncated after residues 483 and 515, were significantly hyperfusogenic compared to wild-type syncytin-1. Cellular and cell-surface expression levels of these two variant proteins were similar to those of wildtype syncytin-1. In testing the latter we found that only a very minor portion of recombinantly expressed cellular syncytin-1 was fully mature and expressed on the cell surface. Our results contribute to the understanding of the structure-funct

Who reads C-Terminal truncations of syncytin-1 (ERVWE1 envelope) that increase its fusogenicity?

Author

Sascha Drewlo; Simone Leyting; Maria Kokozidou; François Mallet; Andy J.G. Pötgens

Publisher

Walter de Gruyter GmbH

Published

2006

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)