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Vaccinia virus G1 protein: absence of autocatalytic self-processing

Authors
  • Leite, F. G. G.1, 2
  • Bergthaler, A.3
  • Skern, T.1
  • 1 Medical University of Vienna, Max F. Perutz Laboratories, Dr. Bohr-Gasse 9/3, Vienna, 1030, Austria , Vienna (Austria)
  • 2 The Francis Crick Institute, Cellular Signalling and Cytoskeletal Function, 1 Midland Road, London, NW1 1AT, UK , London (United Kingdom)
  • 3 CeMM Research Center for Molecular Medicine of the Austrian Academy of Sciences, Lazarettgasse 14, Vienna, 1090, Austria , Vienna (Austria)
Type
Published Article
Journal
Archives of Virology
Publisher
Springer-Verlag
Publication Date
May 18, 2017
Volume
162
Issue
9
Pages
2803–2808
Identifiers
DOI: 10.1007/s00705-017-3409-y
Source
Springer Nature
Keywords
License
Yellow

Abstract

Vaccinia virus relies on a series of proteolytic cleavage events involving two viral proteins, I7 and G1, to complete its life cycle. Furthermore, G1 itself is cleaved during vaccinia virus infection. However, convincing evidence is lacking to show whether G1 participates in autoproteolysis or is a substrate of another protease. We employed both biochemical and cell-based approaches to investigate G1 cleavage. G1, when expressed in bacteria, rabbit reticulocyte lysates or HeLa cells, was not processed. Moreover, G1 was cleaved in infected cells, but only in the presence of virus late gene expression; cleavage was strongly inhibited by proteasome inhibitors. Thus, these results imply a more complex G1 cleavage reaction than previously envisaged.

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