Region-selective and site-specific glycation of influenza proteins surrounding the viral envelope membrane

ABSTRACT: Analysis of protein modifications is critical for quality control of therapeutic biologics. We used highly sensitive LC MS/MS analyses combined with multiple enzyme digestions to determine low abundance early-stage lysine glycation products of influenza vaccines derived from embryonated chicken eggs and cultured cells. A method utilizing chemoselective labeling of glycated lysine residues, through rapid conversion of site-specific glycation to stable N-ethylmaleimide derivatives at mildly acidic conditions, identified highly reactive lysine sites of proteins. As a result, we determined a widespread distribution of lysine modifications attributed by the region-selectivity and site-specificity of glycation toward influenza matrix 1, hemagglutinin and neuraminidase.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Influenza A Virus (a/turkey/italy/3466/1999(h7n1))

SUBMITTER: Yi-Min She  

LAB HEAD: Xu Zhang

PROVIDER: PXD052096 | Pride | 2024-10-17

REPOSITORIES: Pride