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Journal of General Virology, Vol 79, 2023-2025, Copyright © 1998 by Society for General Microbiology

ARTICLES

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

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.


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