{Reference Type}: Journal Article
{Title}: Identification of a novel consensus sequence at the cleavage site of the Lassa virus glycoprotein.
{Author}: Lenz O;ter Meulen J;Feldmann H;Klenk HD;Garten W;
{Journal}: J Virol
{Volume}: 74
{Issue}: 23
{Year}: Dec 2000
{Factor}: 6.549
{DOI}: 10.1128/jvi.74.23.11418-11421.2000
{Abstract}: 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.