Temperature-sensitive mutants of foot-and-mouth disease virus with altered structural polypeptides. I. Identification by electrofocusing.
The structural polypeptides of foot-and-mouth disease virus were analyzed by electrofocusing in a polyacrylamide gel containing 9 M urea. Three versions of the technique were used to accomodate the widely differing isoelectric points of the four polypeptides. VP2 was identified by comparing mature virus with procapsids. The selective actions of proteases on virions of two serotypes and on their 12S particles were examined. From this emerged a simple test for distinguishing the similarly sized polypeptides: VP1, VP2, and VP3. The effects of carbamylation and succinylation on the charge of the polypeptides were investigated. From the properties of polypeptides modified either chemically or by mutation, it was concluded that all amino acid substitutions that might be expected to cause a charge change would be detected except for neutral-to-histidine substitutions in the most basic polypeptide, VP1. In a sample of 73 temperature-sensitive mutants, 11 classes of variant polypeptides were distinguished on the basis of charge. Their molecular weights were unchanged. Alterations were found in all structural polypeptides except VP4. Mutations affecting VP2 caused similar shifts in the precursor, VP0.
D005537:Aphthovirus / Q000032:analysis / Q000235:genetics*; D002213:Capsid / Q000032:analysis / Q000235:genetics*; D007525:Isoelectric Focusing; D007526:Isoelectric Point; D008970:Molecular Weight; D009154:Mutation; D010447:Peptide Hydrolases / Q000494:pharmacology; D010455:Peptides / Q000032:analysis / Q000235:genetics; D013696:Temperature; D014764:Viral Proteins / Q000235:genetics*
D010455:Peptides; D014764:Viral Proteins; D010447:Peptide Hydrolases