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J. Virol. doi:10.1128/JVI.02759-06
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Mapping the landscape of the LCMV stable signal peptide reveals novel functional domains

Department of Molecular and Integrative Neurosciences, The Scripps Research Institute, La Jolla, CA 92037; Department of Microbiology and Immunology, Emory University, Atlanta, GA 30322

^* To whom correspondence should be addressed. Email: buchm{at}scripps.edu.

	Abstract

The stable signal peptide (SSP) of lymphocytic choriomeningitis virus surface glycoprotein precursor (pGPC) has several unique characteristics. The SSP is unusually long at 58 amino acids, contains two hydrophobic domains and its sequence is highly conserved among both Old and New World arenaviruses. To better understand the functions of SSP, a panel of point and deletion mutations was created using in vitro mutagenesis to target the highly conserved elements within SSP. We were also able to confirm critical residues required for separate SSP functions by trans-complementation. Using these approaches, it was possible to resolve functional domains of SSP. In characterizing our SSP mutations we have discovered that SSP is involved in several distinct functions within the viral lifecycle beyond translocation of the viral surface glycoprotein precursor into the endoplasmic reticulum lumen. SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of GP1 and GP2 by SKI-1/S1P protease, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH dependent glycoprotein-mediated cell fusion.

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