Identification of Amino Acid Substitutions in Avian Influenza Virus (H5N1) Matrix Protein 1 by Using Nanoelectrospray MS and MS/MS

Ning Liu, Wenjun Song, Kim Chung Lee, Pui Wang, Honglin Chen*, Zongwei CAI

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)

Abstract

Matrix protein 1 (M1), the major structural protein of the avian influenza virus, plays a critical role in regulation of viral RNA transcription via interaction with RNA and transportation of RNP cores. Mutations in M1 have been frequently observed in the highly virulent avian influenza H5N1 virus, which might be crucial to the pathogenic function. Here we report the characterization of mutated peptides in M1 purified from highly pathogenic avian influenza virus H5N1 by nanoelectrospray MS and MS/MS analyses on a quadrupole-time-of-flight mass spectrometer (Q-TOFMS). The specificity of tandem mass spectrometry allowed the identification of six amino acid (AA) substitutions in M1, including R95K, A166V, I168T, N207S, N224S, and R230K. Two commonly observed modifications such as oxidation and deamidation were accurately assigned in the protein. Bioinformatics analysis suggested some relationship between the amino acid substitution and structural property of M1 protein. Discussions on de novo sequencing of MS/MS spectra, especially in dealing with the AA substitutions, were provided.

Original languageEnglish
Pages (from-to)312-320
Number of pages9
JournalJournal of the American Society for Mass Spectrometry
Volume20
Issue number2
DOIs
Publication statusPublished - Feb 2009

Scopus Subject Areas

  • Structural Biology
  • Spectroscopy

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