Surface modifications of influenza proteins upon virus inactivation by β‐propiolactone
Identifieur interne : 000935 ( Main/Exploration ); précédent : 000934; suivant : 000936Surface modifications of influenza proteins upon virus inactivation by β‐propiolactone
Auteurs : Yi-Min She [Canada] ; Keding Cheng [Canada] ; Aaron Farnsworth [Canada] ; Xuguang Li [Canada] ; Terry D. Cyr [Canada]Source :
- PROTEOMICS [ 1615-9853 ] ; 2013-12.
English descriptors
- Teeft :
- Acid residues, Acylated products, Amino, Amino acid, Amino acid residues, Amino acids, Antigenic, Antigenic epitopes, Antigenic sites, Arginine residues, Canada proteomics, Candidate vaccines, Chem, Chemical reactions, Cysteine, Cysteine residues, Database, Database search, Digestion, Disulphide bonds, Enzymatic activity, False positives, Formaldehyde, Glycoprotein, Glycosylation, Gmbh, Health canada, Hemagglutinin, High mascot scores, Histidine residues, Immune response, Immunogenicity, Inactivation, Information table, Kgaa, Linear gradient, Majesty, Maldi, Manual inspection, Mass error, Mass increase, Mass shift, Mass spectrometer, Mass spectrometry, More sites, Neuraminidase, Nucleobase analogues, Oxidized, Oxidized carbamidomethyl, Pandemic, Peptide, Peptide ions, Peptide sequence, Peptide sequences, Porous graphitic carbon, Propiolactone, Protein, Protein conformation, Protein delipidation, Protein function, Protein palmitoylation, Protein sequence, Protein sequences, Protein structures, Protein sulfenic acids, Proteomic analysis, Proteomics, Quality control, Reagent, Receptor binding, Relative intensity, Residue, Room temperature, Sequence coverage, Side chain, Signal peptide, Steric hindrance, Subtle differences, Surface region, Surface regions, Thermo fisher, Trypsin, Tryptic digests, Tryptic peptides, Uenza viruses, Ultra performance, Unique sites, Uplc, Vaccine, Vaccine antigens, Vaccine evaluation, Vaccine production, Verlag, Verlag gmbh, Viral, Viral proteins, Virus, Virus antigens, Virus inactivation, Virus strains, Weinheim, Weinheim proteomics.
Abstract
Inactivation of intact influenza viruses using formaldehyde or β‐propiolactone (BPL) is essential for vaccine production and safety. The extent of chemical modifications of such reagents on viral proteins needs to be extensively investigated to better control the reactions and quality of vaccines. We have evaluated the effect of BPL inactivation on two candidate re‐assortant vaccines (NIBRG‐121xp and NYMC‐X181A) derived from A/California/07/2009 pandemic influenza viruses using high‐resolution FT‐ICR MS‐based proteomic approaches. We report here an ultra performance LC MS/MS method for determining full‐length protein sequences of hemagglutinin and neuraminidase through protein delipidation, various enzymatic digestions, and subsequent mass spectrometric analyses of the proteolytic peptides. We also demonstrate the ability to reliably identify hundreds of unique sites modified by propiolactone on the surface of glycoprotein antigens. The location of these modifications correlated with changes to protein folding, conformation, and stability, but demonstrated no effect on protein disulfide linkages. In some cases, these modifications resulted in suppression of protein function, an effect that correlated with the degree of change of the modified amino acids’ side chain length and polarity.
Url:
DOI: 10.1002/pmic.201300096
Affiliations:
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The extent of chemical modifications of such reagents on viral proteins needs to be extensively investigated to better control the reactions and quality of vaccines. We have evaluated the effect of BPL inactivation on two candidate re‐assortant vaccines (NIBRG‐121xp and NYMC‐X181A) derived from A/California/07/2009 pandemic influenza viruses using high‐resolution FT‐ICR MS‐based proteomic approaches. We report here an ultra performance LC MS/MS method for determining full‐length protein sequences of hemagglutinin and neuraminidase through protein delipidation, various enzymatic digestions, and subsequent mass spectrometric analyses of the proteolytic peptides. We also demonstrate the ability to reliably identify hundreds of unique sites modified by propiolactone on the surface of glycoprotein antigens. The location of these modifications correlated with changes to protein folding, conformation, and stability, but demonstrated no effect on protein disulfide linkages. In some cases, these modifications resulted in suppression of protein function, an effect that correlated with the degree of change of the modified amino acids’ side chain length and polarity.</div></front></TEI><affiliations><list><country><li>Canada</li></country></list><tree><country name="Canada"><noRegion><name sortKey="She, Yi In" sort="She, Yi In" uniqKey="She Y" first="Yi-Min" last="She">Yi-Min She</name></noRegion><name sortKey="Cheng, Keding" sort="Cheng, Keding" uniqKey="Cheng K" first="Keding" last="Cheng">Keding Cheng</name><name sortKey="Cyr, Terry D" sort="Cyr, Terry D" uniqKey="Cyr T" first="Terry D." last="Cyr">Terry D. Cyr</name><name sortKey="Cyr, Terry D" sort="Cyr, Terry D" uniqKey="Cyr T" first="Terry D." last="Cyr">Terry D. Cyr</name><name sortKey="Cyr, Terry D" sort="Cyr, Terry D" uniqKey="Cyr T" first="Terry D." last="Cyr">Terry D. Cyr</name><name sortKey="Farnsworth, Aaron" sort="Farnsworth, Aaron" uniqKey="Farnsworth A" first="Aaron" last="Farnsworth">Aaron Farnsworth</name><name sortKey="Li, Xuguang" sort="Li, Xuguang" uniqKey="Li X" first="Xuguang" last="Li">Xuguang Li</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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