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- Publisher Website: 10.1021/ac900026f
- Scopus: eid_2-s2.0-66149141008
- PMID: 19402721
- WOS: WOS:000265632400041
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Article: Subtyping of the influenza virus by high resolution mass spectrometry
Title | Subtyping of the influenza virus by high resolution mass spectrometry |
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Authors | |
Issue Date | 2009 |
Citation | Analytical Chemistry, 2009, v. 81, n. 9, p. 3500-3506 How to Cite? |
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. © 2009 American Chemical Society. |
Persistent Identifier | http://hdl.handle.net/10722/250924 |
ISSN | 2023 Impact Factor: 6.7 2023 SCImago Journal Rankings: 1.621 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Schwahn, Alexander B. | - |
dc.contributor.author | Wong, Jason W H | - |
dc.contributor.author | Downard, Kevin M. | - |
dc.date.accessioned | 2018-02-01T01:54:05Z | - |
dc.date.available | 2018-02-01T01:54:05Z | - |
dc.date.issued | 2009 | - |
dc.identifier.citation | Analytical Chemistry, 2009, v. 81, n. 9, p. 3500-3506 | - |
dc.identifier.issn | 0003-2700 | - |
dc.identifier.uri | http://hdl.handle.net/10722/250924 | - |
dc.description.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. © 2009 American Chemical Society. | - |
dc.language | eng | - |
dc.relation.ispartof | Analytical Chemistry | - |
dc.title | Subtyping of the influenza virus by high resolution mass spectrometry | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1021/ac900026f | - |
dc.identifier.pmid | 19402721 | - |
dc.identifier.scopus | eid_2-s2.0-66149141008 | - |
dc.identifier.volume | 81 | - |
dc.identifier.issue | 9 | - |
dc.identifier.spage | 3500 | - |
dc.identifier.epage | 3506 | - |
dc.identifier.isi | WOS:000265632400041 | - |
dc.identifier.issnl | 0003-2700 | - |