Site-specific antibodies define a cleavage site conserved among arenavirus GP-C glycoproteins

M. J. Buchmeier, P. J. Southern, B. S. Parekh, M. K. Wooddell, M. B. Oldstone

Research output: Contribution to journalArticlepeer-review

50 Scopus citations

Abstract

Arenaviruses share a common strategy for glycoprotein synthesis and processing in which a mannose-rich precursor glycoprotein, termed GP-C in lymphocytic choriomeningitis virus (LCMV), is posttranslationally processed by oligosaccharide trimming and proteolytic cleavage to yield two structural glycoproteins, GP-1 and GP-2. Mapping the orientation and proteolytic cleavage site(s) in such polyproteins has traditionally required direct protein sequencing of one or more of the cleaved products. This technique requires rigorous purification of the products for sequencing and may be complicated by amino-terminal modifications which interfere with sequence analysis. We used an alternative approach in which synthetic peptides corresponding to sequences bracketing a potential protease cleavage site were used to raise antisera which define the boundaries of the cleaved products. We found that cleavage of LCMV GP-C to yield GP-1 and GP-2 occurs within a 9-amino-acid stretch of GP-C which contains a paired basic amino acid group -Arg-Arg-, corresponding to amino acids 262 to 263 in the LCMV GP-C sequence. By comparison with the predicted amino acid sequences of a second LCMV strain, LCMV-WE, as well as with the deduced amino acid sequences of the New World arenavirus Pichinde and the Old World virus Lassa, we observed similar conservation of paired basic and flanking amino acid sequences among these viruses.

Original languageEnglish (US)
Pages (from-to)982-985
Number of pages4
JournalJournal of virology
Volume61
Issue number4
DOIs
StatePublished - 1987

Fingerprint

Dive into the research topics of 'Site-specific antibodies define a cleavage site conserved among arenavirus GP-C glycoproteins'. Together they form a unique fingerprint.

Cite this