Sequencing, genomic localization and initial characterization of the VPg of pea enation mosaic enamovirus

• Published in: Journal of general virology Vol. 79; no. 8; pp. 2023 - 2025
• Main Authors: Wobus, CE, Skaf, JS, Schultz, MH, de Zoeten, GA
• Format: Journal Article
• Language: English
• Published: England Soc General Microbiol 01-08-1998
• Subjects: Amino Acid Sequence; Chromosome Mapping; Luteovirus - genetics; Molecular Sequence Data; Pisum sativum - virology; Viral Core Proteins - genetics
• ISSN: 0022-1317; 1465-2099
• DOI: 10.1099/0022-1317-79-8-2023

CE Wobus, JS Skaf, MH Schultz and GA de Zoeten
Department of Botany and Plant Pathology, Michigan State University, East Lansing 48824, USA.
The amino acid sequence of the genome-linked viral protein (VPg) of pea
enation mosaic enamovirus (PEMV) has been determined. The VPg is encoded by
nt 1811-1894 within ORF1 of RNA1 downstream of the proteinase motif. Direct
N terminus sequencing of intact and endoproteinase Asp-N-digested VPg
combined with electrospray mass spectroscopy confirmed that the VPg is
composed of 28 amino acids with a molecular mass of 3138 Da. The context of
the N and C terminus residues as well as the position and size of the VPg
suggest that the mature VPg may be generated via post-translational
proteolytic processing of the polyprotein arrangement of membrane
anchor-proteinase- VPg-polymerase encoded by ORFs 1 and 2. Computer
comparisons did not reveal any significant similarity between the VPg of
PEMV and any other sequences including those of the VPgs of related
subgroup II luteoviruses.