Proteomics

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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

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

She Yi-Min YM   Jia Zongchao Z   Zhang Xu X  

Scientific reports 20240816 1


Analysis of protein modifications is critical for quality control of therapeutic biologics. However, the identification and quantification of naturally occurring glycation of membrane proteins by mass spectrometry remain technically challenging. 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. Straightforward sequencin  ...[more]

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