Journal
VIROLOGY
Volume 522, Issue -, Pages 260-270Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2018.07.010
Keywords
Picornavirus; Polyprotein; Virus assembly; Protease cleavage site; Structural proteins
Categories
Funding
- National Veterinary Institute within the Technical University of Denmark
- Danish Council for Independent Research/Natural Sciences [1323-00117B]
- BBSRC [BBS/E/I/00007034] Funding Source: UKRI
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The foot-and-mouth disease virus capsid precursor, P1-2A, is cleaved by the 3C protease (3C(Pro)) to VPO, VP3, VP1 and 2A. The P1-2A precursor (wt or mutant) was expressed alone or with 3C(Pro) and processing of P1-2A was determined. The VP2 K217R and VP3 I2P substitutions (near the VP0/VP3 junction) strongly reduced the processing at this junction by 3C(Pro) while the substitution VP2 K217E blocked cleavage. At the VP3/VP1 junction, the substitutions VP3 Q2221P and VP1 T1P each severely inhibited processing at this site. Blocking cleavage at either junction did not prevent processing elsewhere in P1-2A. These modifications were also introduced into full-length FMDV RNA; only wt and the VP2 K217R mutant were viable. Uncleaved VPO-VP3 and the processed products were observed within cells infected with the mutant virus. The VPO-VP3 was not incorporated into empty capsids or virus particles. The three junctions within P1-2A are processed by 3C(Pro) independently.
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