Myristoylation of foot-and-mouth disease virus capsid protein precursors is independent of other viral proteins and occurs in both mammalian and insect cells.
نویسندگان
چکیده
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.
منابع مشابه
Nucleotide Sequence of Gene Encoding Capsid Protein VPI of Foot-and-Mouth Disease Virus / Type O1 Iran
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عنوان ژورنال:
- The Journal of general virology
دوره 72 ( Pt 3) شماره
صفحات -
تاریخ انتشار 1991