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Myristoylation of foot-and-mouth disease virus capsid protein precursors is independent of other viral proteins and occurs in both mammalian and insect cells.

作者信息

Belsham G J, Abrams C C, King A M, Roosien J, Vlak J M

机构信息

AFRC Institute for Animal Health, Pirbright Laboratory, Woking, Surrey, U.K.

出版信息

J Gen Virol. 1991 Mar;72 ( Pt 3):747-51. doi: 10.1099/0022-1317-72-3-747.

DOI:10.1099/0022-1317-72-3-747
PMID:1848606
Abstract

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.

摘要

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