Strain identification of commercial influenza vaccines by mass spectrometry

Analytical Biochemistry

Volumn 406, Issue 2, 2010, Pages 193-203

  Creskey, Marybeth C ^a   Smith, Daryl G S ^a   Cyr, Terry D ^a  

^a Health Canada and World Health Organization Collaborating Center for Standardization and Evaluation of Biologicals   (Canada)

Author keywords

Influenza vaccine; Mass spectrometry; Strain identification

Indexed keywords

LIQUID CHROMATOGRAPHY; MANUFACTURE; MASS SPECTROMETRY; PROTEINS; STRAIN; TESTING;

INFLUENZA VACCINES; LIQUID CHROMATOGRAPHY-MASS SPECTROMETRY; MANUFACTURING PROCESS; PANDEMIC INFLUENZA; PROTEIN SEQUENCING; RAPID TESTING; SEQUENCE COVERAGES; STRAIN IDENTIFICATION;

VACCINES;

ALPHA ACTIN; ALPHA GLOBIN; ALPHA TROPOMYOSIN; ALPHA TUBULIN; APOLIPOPROTEIN A1; APOLIPOPROTEIN B; BETA GLOBIN; BETA TUBULIN; CA 125 ANTIGEN; CALMODULIN; CHYMOTRYPSIN; CLUSTERIN; CYTOKERATIN 19; EPSILON GLOBIN; GLYCOPEPTIDASE; HEMAGGLUTININ; HISTONE H2A; HISTONE H2B; INFLUENZA VACCINE; LIPOCORTIN 2; LIPOPROTEIN; LYSOZYME; OVOMUCOID; RADIXIN; SIALIDASE; TRIPLE VACCINE; TRYPSIN; UNINDEXED DRUG; UROPLAKIN; VACCINE;

AMINO ACID SEQUENCE; ARTICLE; DATA BASE; FILTER; MASS FRAGMENTOGRAPHY; MASS SPECTROMETRY; PRIORITY JOURNAL; STRAIN IDENTIFICATION; VIRUS STRAIN;

EID: 77956231586     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2010.07.016     Document Type: Article

References (29)

1. World Health Organization, Influenza (seasonal), http://www.who.int/mediacentre/factsheets/fs211/en.
2. Drake J. Rates of spontaneous mutation among RNA viruses. Proc. Natl. Acad. Sci. USA 1993, 90:4171-4175.
3. Schild G.C., Wood J.M., Newman R.W. A single-radial-immunodiffusion technique for the assay of influenza haemagglutinin antigen. Bull. World Health Org. 1975, 52:223-229.
4. Wood J.M., Schild G.C., Newman R.W., Seagroatt V. An improved single-radial-immunodiffusion technique for the assay of influenza haemagglutinin antigen: application for potency determination of inactivated whole virus and subunit vaccines. J. Biol. Stand. 1977, 5:237-247.
5. Wood J.M., Mumford J., Schild G.C., Webster R.G., Nicholson K.G. Single-radial-immunodiffusion potency tests of inactivated influenza vaccines for use in man and animals. Dev. Biol. Stand. 1985, 64:169-177.
6. Williams M.S. Single-radial-immunodiffusion as an in vitro potency assay for human inactivated viral vaccines. Vet. Microbiol. 1993, 37:253-262.
7. Hilleman M. Realities and enigmas of human viral influenza: pathogenesis, epidemiology, and control. Vaccine 2002, 20:3068-3087.
8. Vester D., Rapp E., Gade D., Genzel Y., Reichl U. Quantitative analysis of cellular proteome alterations in human influenza A virus-infected mammalian cell lines. Proteomics 2009, 12:3316-3327.
9. García-Cañas V., Lorbetskie B., Girard M. Rapid and selective characterization of influenza virus constituents in monovalent and multivalent preparations using non-porous reversed-phase high performance liquid chromatography columns. J. Chromatogr. 2006, 1123:225-232.
10. García-Cañas V., Lorbetskie B., Bertrand D., Cyr T.D., Girard M. Selective and quantitative detection of influenza virus proteins in commercial vaccines using two-dimensional high-performance liquid chromatography and fluorescence detection. Anal. Chem. 2007, 79:3164-3172.
11. Kapteyn J.C., Saidi M.D., Dijkstra R., Kars C., Tjon J.C., Weverling G.J., de Vocht M.L., Kompier R., van Montfort B.A., Guichoux J.Y., Goudsmit J., Lagerwerf F.M. Haemagglutinin quantification and identification of influenza A and B strains propagated in PER.C6 cells: a novel RP-HPLC method. Vaccine 2006, 24:3137-3144.
12. Schwann A.B., Wong J.W., Downard K.M. Subtyping of the influenza virus by high resolution mass spectrometry. Anal. Chem. 2009, 81:3500-3506.
13. Schwann A.B., Wong J.W., Downard K.M. Typing of human and animal strains of influenza virus, with conserved signature peptides of matrix M1 protein, by high resolution mass spectrometry. J. Virol. Methods 2010, 165:178-185.
14. Schwarzer J., Rapp E., Reichl U. N-Glycan analysis by CGE-LIF Profiling influenza A virus hemagglutinin N-glycosylation during vaccine production. Electrophoresis 2008, 29:4203-4214.
15. Bao Y., Bolotov P., Dernovoy D., Kiryutin B., Zaslavsky L., Tatusova T., Ostell J., Lipman D. The influenza virus resource at the National Center for Biotechnology Information. J. Virol. 2008, 82:596-601.
16. Air G.M. Nucleotide sequence coding for the " signal peptide" and N terminus of the hemagglutinin from an Asian (H2N2) strain of influenza virus. Virology 1979, 97:468-472.
17. Manza L.L., Stamer S.L., Ham A.J., Codreanu S.G., Liebler D.C. Sample preparation and digestion for proteomic analyses using spin filters. Proteomics 2005, 5:1742-1745.
18. Wiśniewski J.R., Zougman A., Nagaraj N., Mann M. Universal sample preparation method for proteome analysis. Nat. Methods 2009, 6:359-363.
19. Wang N., Li L. Exploring the precursor ion exclusion feature of liquid chromatography-electrospray ionization quadrupole time-of-flight mass spectrometry for improving protein identification in shotgun proteome analysis. Anal. Chem. 2008, 80:4696-4710.
20. Bendall S.C., Hughes C., Campbell J.L., Stewart M.H., Pittock P., Liu S., Bonneil E., Thibault P., Bhatia M., Lajoie G.A. An enhanced mass spectrometry approach reveals human embryonic stem cell growth factors in culture. Mol. Cell. Proteomics 2009, 8:421-432.
21. Harvey D.J. Proteomic analysis of glycosylation: structural determination of N- and O-linked glycans by mass spectrometry. Expert Rev. Proteomics 2005, 2:87-101.
22. 18 O-labeled water. Anal. Biochem. 1992, 205:151-158.
23. Tsur D., Tanner S., Zandi E., Bafna V., Pevzner P.A. Identification of post-translational modifications by blind search of mass spectra. Nat. Biotechnol. 2005, 23:1562-1567.
24. Alves P., Arnold R.J., Clemmer D.E., Li Y., Reilly J.P., Sheng O., Tang H., Xun Z., Zeng R., Radivojac P. Fast and accurate identification of semi-tryptic peptides in shotgun proteomics. Bioinformatics 2008, 24:102-109.
25. Strader M.B., Tabb D.L., Hervey W.J., Pan C., Hurst G.B. Efficient and specific trypsin digestion of microgram to nanogram quantities of proteins in organic-aqueous solvent systems. Anal. Chem. 2006, 78:125-134.
26. Steinhauer D.A. Role of hemagglutinin cleavage for the pathogenicity of influenza virus. Virology 1999, 258:1-20.
27. Both G.W., Shi C.H., Kilbourne E.D. Hemagglutinin of swine influenza virus: a single amino acid change pleiotropically affects viral antigenicity and replication. Proc. Natl. Acad. Sci. USA 1983, 80:6996-7000.
28. Kilbourne E.D., Taylor A.H., Whitaker C.W., Sahai R., Caton A.J. Hemagglutinin polymorphism as the basis for low- and high-yield phenotypes of swine influenza virus. Proc. Natl. Acad. Sci. USA 1988, 85:7782-7785.
29. Tumpey T.M., Maines T.R., Van Hoeven N., Glaser L., Solorzano A., Pappas C., Cox N.J., Swayne D.E., Palese P., Katz J.M., Garcia-Sastre A. A two-amino acid change in the hemagglutinin of the 1918 influenza virus abolishes transmission. Science 2007, 315:655-659.