Myristoylation of foot-and-mouth disease virus capsid protein precursors is independent of other viral proteins and occurs in both mammalian and insect cells.
The myristoylation of the foot-and-mouth disease virus (FMDV) capsid precursor P1-2A and its amino-terminal cleavage product 1AB, expressed from subgenomic cDNA, has been analysed. The modification reaction is independent of other FMDV proteins and occurs in both mammalian and insect cells. Blocking of the myristoylation site does not prevent efficient processing of the FMDV capsid precursor. A cDNA cassette in which the leader protease sequence is substituted by an ATG codon produces myristoylated 1AB, indicating correct removal of the novel N-terminal methionine residue.
Belsham
G J
GJ
AFRC Institute for Animal Health, Pirbright Laboratory, Woking, Surrey, U.K.
Abrams
C C
CC
King
A M
AM
Roosien
J
J
Vlak
J M
JM
D000595:Amino Acid Sequence; D000818:Animals; D005537:Aphthovirus / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D002213:Capsid / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002460:Cell Line; D004591:Electrophoresis, Polyacrylamide Gel; D007313:Insecta; D008322:Mammals; D008969:Molecular Sequence Data; D009226:Myristates / Q000378:metabolism*; D009838:Oligodeoxyribonucleotides; D011233:Precipitin Tests; D011498:Protein Precursors / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D014162:Transfection
D009226:Myristates; D009838:Oligodeoxyribonucleotides; D011498:Protein Precursors