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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

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

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

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1437-4315
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Volume 387, Issue 8 (Aug 2006)

Issues

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

Sascha Drewlo
  • Institute of Anatomy II, University Hospital, Wendlingweg 2, RWTH Aachen, D-52057 Aachen, Germany
  • Other articles by this author:
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/ Simone Leyting
  • Institute of Anatomy II, University Hospital, Wendlingweg 2, RWTH Aachen, D-52057 Aachen, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Maria Kokozidou
  • Institute of Anatomy II, University Hospital, Wendlingweg 2, RWTH Aachen, D-52057 Aachen, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ François Mallet
  • UMR 2714, CNRS-bioMérieux IFR 128, BioSciences Lyon-Gerland, Ecole Normale Supérieure de Lyon, F-69364 Lyon, France
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Andy J.G. Pötgens
  • Institute of Anatomy II, University Hospital, Wendlingweg 2, RWTH Aachen, D-52057 Aachen, Germany
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  • De Gruyter OnlineGoogle Scholar
Published Online: 2006-08-09 | DOI: https://doi.org/10.1515/BC.2006.137

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

About the article

Corresponding author


Received: January 25, 2006

Accepted: May 9, 2006

Published Online: 2006-08-09

Published in Print: 2006-08-01


Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2006.137.

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[4]
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