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

Overview

Journal J Virol

Publisher American Society for Microbiology

Date 2003 Feb 14

PMID 12584310

Citations 130

Authors

Winfried R Beyer

Dennis Popplau

Wolfgang Garten

Dorothee von Laer

Oliver Lenz

Affiliations

Soon will be listed here.

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.

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