Jk. Lewis et al., IDENTIFICATION OF VIRAL MUTANTS BY MASS-SPECTROMETRY, Proceedings of the National Academy of Sciences of the United Statesof America, 95(15), 1998, pp. 8596-8601
A method to identify mutations of virus proteins by using protein mass
mapping is described, Comparative mass mapping was applied to a struc
tural protein of the human rhinovirus Cys1199 --> Tyr mutant and to ge
netically engineered mutants of tobacco mosaic virus. The information
generated from this approach can rapidly identify the peptide or prote
in containing the mutation and, in cases when nucleic acid sequencing
is required, significantly narrows the region of the genome that must
be sequenced. High-resolution matrix-assisted laser desorption/ionizat
ion (MALDI) mass spectrometry and tandem mass spectrometry were used t
o identify amino acid substitutions. This method provides valuable inf
ormation for those analyzing viral variants and, in some cases, offers
a rapid and accurate alternative to nucleotide sequencing.