Identification of a novel consensus sequence at the cleavage site of the Lassa virus glycoprotein.
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 GTF(262) when analyzed by Edman degradation. Upstream of this site, GP-C contains the tetrapeptide sequence RRLL(259), 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)-L(259) (where X stands for L, I, or V) is essential for cleavage of the peptide bond between leucine(259) and glycine(260). 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.
Lenz
O
O
Institut für Virologie, D-35037 Marburg, Germany.
ter Meulen
J
J
Feldmann
H
H
Klenk
H D
HD
Garten
W
W
D000595:Amino Acid Sequence; D016384:Consensus Sequence; D007836:Lassa virus / Q000737:chemistry*; D008562:Membrane Glycoproteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D014759:Viral Envelope Proteins / Q000737:chemistry*
D008562:Membrane Glycoproteins; D014759:Viral Envelope Proteins