Journal
JOURNAL OF VIROLOGY
Volume 82, Issue 9, Pages 4656-4659Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.02077-07
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Funding
- Austrian Science Fund FWF [P 17988] Funding Source: Medline
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The foot-and-mouth disease virus (FMDV) leader proteinase (L-pro) self-processes inefficiently at the L-pro/VP4 cleavage site LysLeuLys*GlyAlaGly (* indicates cleaved peptide bond) when the leucine at position P2 is replaced by phenylalanine. Molecular modeling and energy minimization identified the L-pro residue L143 as being responsible for this discrimination. The variant L-pro L143A self-processed efficiently at the L-pro/VP4 cleavage site containing P2 phenylalanine, whereas the L143M variant did not. L-pro L143A self-processing at the eIF4GII sequence AspPbeGly*ArgGlnThr was improved but showed more-extensive aberrant processing. Residue 143 in L-pro is occupied only by leucine and methionine in all sequenced FMDV serotypes, implying that these bulky side chains are one determinant of the restricted specificity of L-pro.
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