The N-terminal region (VP4) of the foot-and-mouth disease capsid precursor (P1-2A) is not required during its synthesis to allow subsequent processing by the 3C protease

Thea Kristensen, Preben Normann, Graham J. Belsham*

*Corresponding author af dette arbejde

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningpeer review

1 Citationer (Scopus)
26 Downloads (Pure)

Abstract

The capsid precursor (P1-2A) of foot-and-mouth disease virus is processed by the 3C protease (3Cpro) to VP0, VP3 and VP1 plus 2A. During capsid assembly, the VP0 is cleaved to VP4 plus VP2. Single amino acid changes in a conserved motif (YCPRP) near the C-terminus of VP1 can block processing of the capsid precursor by the 3Cpro, although the cleavage sites are located hundreds of amino acids distant from this motif, presumably due to misfolding. In contrast, we show here that the absence of the VP4 sequence during the synthesis of the capsid precursor does not affect its subsequent processing. Cleavage of this truncated precursor by 3Cpro at the VP3/VP1 and VP2/VP3 junctions occurred efficiently. Thus, in contrast to the presence of the YCPRP motif in VP1, there are no critical motifs near the N-terminus of the precursor, within VP4, required for correct cleavage by 3Cpro.

OriginalsprogEngelsk
TidsskriftVirology
Vol/bind570
Sider (fra-til)29-34
Antal sider6
ISSN0042-6822
DOI
StatusUdgivet - 2022

Bibliografisk note

Funding Information:
We thank Karl Ljungberg (Karolinska Institutet) for kindly providing the DREP vector and Santina Grazioli (IZSLER, Brescia) for the anti-FMDV VP2 (5B2) monoclonal antibody.

Publisher Copyright:
© 2022 The Authors

Citationsformater