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Journal of Virology, April 2007, p. 3187-3197, Vol. 81, No. 7
0022-538X/07/$08.00+0     doi:10.1128/JVI.02465-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Targeting of the Sendai Virus C Protein to the Plasma Membrane via a Peptide-Only Membrane Anchor

Department of Microbiology and Molecular Medicine, University of Geneva School of Medicine, 11 Ave de Champel, CH1211 Geneva, Switzerland

Received 9 November 2006/ Accepted 7 January 2007

Several cellular proteins are synthesized in the cytosol on free ribosomes and then associate with membranes due to the presence of short peptide sequences. These membrane-targeting sequences contain sites to which lipid chains are attached, which help direct the protein to a particular membrane domain and anchor it firmly in the bilayer. The intracellular concentration of these proteins in particular cellular compartments, where their interacting partners are also concentrated, is essential to their function. This paper reports that the apparently unmodified N-terminal sequence of the Sendai virus C protein (MPSFLKKILKLRGRR . . .; letters in italics represent hydrophobic residues; underlined letters represent basic residues, which has a strong propensity to form an amphipathic -helix in a hydrophobic environment) also function as a membrane targeting signal and membrane anchor. Moreover, the intracellular localization of the C protein at the plasma membrane is essential for inducing the interferon-independent phosphorylation of Stat1 as part of the viral program to prevent the cellular antiviral response.

Published ahead of print on 17 January 2007.

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