Open AccessEndoproteolytic Processing of the Lymphocytic Choriomeningitis Virus Glycoprotein by the Subtilase SKI-1/S1P
Author(s) -
Winfried Beyer,
Dennis Pöpplau,
Wolfgang Garten,
Dorotheé von Laer,
Oliver Lenz
Publication year - 2003
Publication title -
journal of virology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.617
H-Index - 292
eISSN - 1070-6321
pISSN - 0022-538X
DOI - 10.1128/jvi.77.5.2866-2872.2003
Subject(s) - lymphocytic choriomeningitis , biology , arenavirus , virology , glycoprotein , infectivity , virus , cleavage (geology) , microbiology and biotechnology , genetics , cytotoxic t cell , in vitro , paleontology , fracture (geology)
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.