Mengo virus maturation is accompanied by C-terminal modification of capsid protein VP1.
We have demonstrated that the C-terminal ends of the VP1 proteins of Mengo virus undergo a postassembly trimming of three amino acid residues. A variable proportion of the VP1 molecules isolated from purified virions terminate at Glu 277, which corresponds to the initial viral protease 3C cleavage site. The remainder of the VP1 molecules terminates at Leu 274. When chymotrypsin treatment is included in the virus purification procedure, Leu 274 is the exclusive C-terminal amino acid of the VP1 molecules. The trimming process was found to influence the pH-mediated dissociability of virions in vitro: this was demonstrated by sucrose gradient analysis and electron microscopy. Since long-term incubation of purified virions did not alter the C-terminal Glu 277/Leu 274 ratio, it appears that the trimming process is not autocatalytic.
Boege
U
U
Department of Biochemistry, University of Alberta, Edmonton, Canada.
Scraba
D G
DG
D002213:Capsid / Q000378:metabolism*; D002918:Chymotrypsin / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D008574:Mengovirus / Q000254:growth & development / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
D002918:Chymotrypsin