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Papers In Press, published online ahead of print March 26, 2001
Physics & Astronomy, University of Manitoba, Winnipeg, MB R3T 2N2
Corresponding Author: standin{at}cc.umanitoba.ca
Time-of-flight mass spectrometry (TOFMS) has been applied to determine the complete coat protein amino-acid sequences of a number of distinct brome mosaic virus (BMV) isolates. Ionization was carried out by both electrospray ionization (ESI) and matrix-assisted laser desorption/ionization (MALDI). After determining overall coat protein masses, the proteins were digested with trypsin or Lys-C proteinases, and the digestion products analyzed in a MALDI QqTOF mass spectrometer. The N-terminus of the coat protein was found to be acetylated in each BMV isolate analyzed. In one isolate (BMV-Valverde), the amino acid sequence was identical with that predicted from the cDNA sequence of the "type" isolate, but deviations from the predicted amino acid sequence were observed for all the other isolates analyzed. When isolates were propagated in different host taxa, modified coat protein sequences were observed in some cases, along with the original sequence. Sequencing by TOFMS may therefore provide a basis, at the molecular level, for monitoring the effects of host passaging on a virus. Such TOFMS-based analyses assess the complete profiles of coat protein sequences actually present in infected tissues. They are therefore not subject to the selection biases inherent in deducing such sequences from reverse-transcribed and cloned viral RNA.
J. Biol. Chem, 10.1074/jbc.M100189200
Submitted on January 9, 2001
Revised on March 21, 2001
Accepted on March 26, 2001
Determination of the complete amino acid sequence for the coat protein of brome mosaic virus by time-of-flight mass spectrometry: Evidence for mutations associated with change of propagation host
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