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Journal of Virology, March 2003, p. 2866-2872, Vol. 77, No. 5
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.5.2866-2872.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

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

Winfried R. Beyer,1* Dennis Pöpplau,1 Wolfgang Garten,2 Dorothee von Laer,3 and Oliver Lenz2

Heinrich-Pette-Institut für Experimentelle Virologie und Immunologie an der Universität Hamburg, D-20251 Hamburg,1 Institut für Virologie, Philipps Universität, 35037 Marburg,2 Georg-Speyer-Haus, 60596 Frankfurt, Germany3

Received 1 July 2002/ Accepted 24 October 2002

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.

* Corresponding author. Mailing address: Heinrich-Pette-Institut, Martinistr. 52, D-20251 Hamburg, Germany. Phone: 49 40-8051-270. Fax: 49 40-48051-187. E-mail: beyer{at}hpi.uni-hamburg.de.

Journal of Virology, March 2003, p. 2866-2872, Vol. 77, No. 5
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.5.2866-2872.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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