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J. Biol. Chem., Vol. 278, Issue 43, 41914-41920, October 24, 2003

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Long-lived Signal Peptide of Lymphocytic Choriomeningitis Virus Glycoprotein pGP-C^*

Marc Froeschke, Michael Basler, Marcus Groettrup, and Bernhard Dobberstein¶

From the Zentrum für Molekulare Biologie der Universität Heidelberg, Im Neuenheimer Feld 282, D-69120 Heidelberg and the University of Constance, Department of Immunology, Universitätsstrasse 10, D-78457 Konstanz, Germany

Signal peptides (SPs) direct nascent secretory and membrane proteins to the membrane of the endoplasmic reticulum. They are usually cleaved from the nascent polypeptide by signal peptidase and then further proteolytically processed. The SP of the pre-glycoprotein (pGP-C) of the lymphocytic choriomeningitis virus SP^GP-C (signal peptide of pGP-C) shows different properties: 1) The SP^GP-C is unusually long (58 amino acid residues) and contains two hydrophobic segments interrupted by a lysine residue. 2) The SP^GP-C is cleaved only from a subset of pGP-C proteins. A substantial portion of pGP-C accumulates that still contains the SP^GP-C.3)The cleaved SP^GP-C is rather long-lived (t of more than 6 h). 4) The cleaved SP^GP-C resides in the membrane and is resistant to digestion with proteinase K even in the presence of detergents, suggesting a very compact structure. 5) SP^GP-C accumulates in virus particles. These unusual features of the cleaved SP^GP-C suggest that SP^GP-C not only targets the nascent pGP-C to the endoplasmic reticulum membrane but also has additional functions in lymphocytic choriomeningitis virus life cycle.

Received for publication, March 6, 2003 , and in revised form, July 15, 2003.

^* This work was funded by the Deutsche Forschungsgemeinschaft Grant SFB 352/B1 (to B. D.) and Grant 31-52284 from the Swiss National Science foundation (to M. G.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplementary figures 1S–3S showing Western blot analysis of supernatant and pellet fractions after cell fractionation, Western blot analysis of L929 cells and purified virus particles, and sequence alignment of the predicted signal sequences of some arenavirus glycoproteins.

^¶ To whom correspondence should be addressed: Tel.: 49-6221-546825; Fax: 49-6221-545892; E-mail: dobberstein{at}zmbh.uni-heidelberg.de.

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