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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred


SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751
Impact per Publication (IPP) 2015: 2.609

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1437-4315
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C-Terminal truncations of syncytin-1 (ERVWE1 envelope) that increase its fusogenicity

Sascha Drewlo1 / Simone Leyting2 / Maria Kokozidou3 / François Mallet4 / Andy J.G. Pötgens5

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Corresponding author

Citation Information: Biological Chemistry. Volume 387, Issue 8, Pages 1113–1120, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2006.137, August 2006

Publication History

Received:
January 25, 2006
Accepted:
May 9, 2006
Published Online:
2006-08-09

Abstract

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 wild-type 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-function relationship of syncytin-1, and might have implications for the use of this molecule in gene therapy.

Keywords: cell-cell fusion; cytoplasmic domain; HERV-W; maturation; surface expression

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[1]
Kent Søe, Anne-Sofie Hobolt-Pedersen, and Jean-Marie Delaisse
Bone, 2015, Volume 73, Page 181
[2]
M. Kokozidou, S. Drewlo, C. Bartz, G. Raven, L.O. Brandenburg, C.J. Wruck, and T. Pufe
Annals of Anatomy - Anatomischer Anzeiger, 2011, Volume 193, Number 2, Page 142
[3]
Kent Søe, Thomas L. Andersen, Anne-Sofie Hobolt-Pedersen, Bolette Bjerregaard, Lars-Inge Larsson, and Jean-Marie Delaissé
Bone, 2011, Volume 48, Number 4, Page 837
[4]
Lars-Inge Larsson, Bolette Bjerregaard, and Jan Fredrik Talts
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