Endoproteolytic Processing of the Lymphocytic Choriomeningitis Virus Glycoprotein by the Subtilase SKI-1/S1P

Author:

Beyer Winfried R.1,Pöpplau Dennis1,Garten Wolfgang2,von Laer Dorothee3,Lenz Oliver2

Affiliation:

1. Heinrich-Pette-Institut für Experimentelle Virologie und Immunologie an der Universität Hamburg, D-20251 Hamburg

2. Institut für Virologie, Philipps Universität, 35037 Marburg

3. Georg-Speyer-Haus, 60596 Frankfurt, Germany

Abstract

ABSTRACT The envelope glycoprotein (GP) of lymphocytic choriomeningitis virus (LCMV) is posttranslationally cleaved into two subunits. We show here that this endoproteolytic processing is not required for transport to the cell surface but is essential for LCMV GP to mediate infectivity of pseudotyped retroviral vectors. By systematic mutational analysis of the LCMV GP cleavage site, we determined that the consensus motif R-(R/K/H)-L-(A/L/S/T/F) 265 is essential for the endoproteolytic processing. In agreement with the identified consensus motif, we show that the cellular subtilase SKI-1/S1P cleaves LCMV GP.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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