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Journal of Virology, December 2000, p. 11418-11421, Vol. 74, No. 23
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Identification of a Novel Consensus Sequence at the Cleavage Site of the Lassa Virus Glycoprotein

Oliver Lenz,1 Jan ter Meulen,2 Heinz Feldmann,3 Hans-Dieter Klenk,1 and Wolfgang Garten1,*

Institut für Virologie, D-35037 Marburg,1 and Bernhard-Nocht-Institut für Tropenmedizin, D-20359 Hamburg,2 Germany, and Health Canada, Laboratory Centre for Disease Control, Winnipeg, Manitoba R3E3R2, Canada3

Received 19 June 2000/Accepted 6 September 2000

The Lassa virus glycoprotein consists of an amino-terminal and a carboxy-terminal cleavage fragment designated GP-1 and GP-2, respectively, that are derived by proteolysis from the precursor GP-C. The membrane-anchored GP-2 obtained from purified virions of the Josiah strain revealed the N-terminal tripeptide GTF262 when analyzed by Edman degradation. Upstream of this site, GP-C contains the tetrapeptide sequence RRLL259, which is conserved in all Lassa virus isolates published to date. Systematic mutational analysis of vector-expressed GP-C revealed that the motif R-X (L/I/V)-L259 (where X stands for L, I, or V) is essential for cleavage of the peptide bond between leucine259 and glycine260. This cleavage motif is homologous to the consensus sequence recognized by a novel class of cellular endoproteases which have so far not been implicated in the processing of viral glycoproteins.

* Corresponding author. Mailing address: Institut für Virologie, Robert-Koch-Strasse 17, D-35037 Marburg, Germany. Phone: 49-6421-286-5145. Fax: 49-6421-286-8962. E-mail: garten{at}mailer.uni-marburg.de.

Journal of Virology, December 2000, p. 11418-11421, Vol. 74, No. 23
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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