Subtyping of the influenza virus by high resolution mass spectrometry

Anal Chem. 2009 May 1;81(9):3500-6. doi: 10.1021/ac900026f.

Abstract

High resolution, high mass accuracy mass spectra of hemagglutinin and whole virus digests of influenza are shown to be able to be used to type and subtype the major circulating forms of the virus in humans. Conserved residues and peptide segments of the hemagglutinin antigen have been identified across type A and B strains, and for type B strains of the Yamagata 16/88 and Victoria 2/87 lineages. The theoretical masses for the protonated peptide ions for tryptic peptides of conserved sequence were subsequently shown to be unique in mass when compared to in silico generated peptides from all influenza viral protein sequences and those proteins known to contaminate virus preparations. The approach represents a more rapid and direct approach with which to type and subtype the virus that is of critical need to prepare strategies and treatments in the event of a local epidemic or global pandemic.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Antigens, Viral / chemistry
  • Antigens, Viral / metabolism
  • Conserved Sequence
  • Databases, Genetic
  • Hemagglutinin Glycoproteins, Influenza Virus / chemistry
  • Hemagglutinin Glycoproteins, Influenza Virus / metabolism
  • Humans
  • Influenza A virus / classification*
  • Influenza A virus / immunology
  • Influenza A virus / metabolism
  • Influenza B virus / classification*
  • Influenza B virus / immunology
  • Influenza B virus / metabolism
  • Peptides / analysis
  • Peptides / chemistry
  • Peptides / metabolism
  • Sequence Alignment
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
  • Time Factors
  • Trypsin / metabolism

Substances

  • Antigens, Viral
  • Hemagglutinin Glycoproteins, Influenza Virus
  • Peptides
  • Trypsin