Dataset Information

Topological N-glycosylation and site-specific N-glycan sulfation of influenza proteins in the highly expressed H1N1 candidate vaccines

ABSTRACT: The outbreak of a pandemic influenza H1N1 in 2009 required the rapid generation of high-yielding vaccines against the A/California/7/2009 virus, which were achieved by either addition or deletion of a glycosylation site in the influenza proteins hemagglutinin and neuraminidase. In this report, we have systematically evaluated the glycan composition, structural distribution and topology of glycosylation for two high-yield candidate reassortant vaccines (NIBRG-121xp and NYMC-X181A) by combining various enzymatic digestions with high performance liquid chromatography and multiple-stage mass spectrometry. Proteomic data analyses of the full-length protein sequences determined 9 N-glycosylation sites of hemagglutinin, and defined 6 N-glycosylation sites and the glycan structures of low abundance neuraminidase, which were occupied by high-mannose, hybrid and complex-type N-glycans. A total of ~300 glycopeptides were analyzed and manually validated by tandem mass spectrometry. The unique N-glycan structure and topological location of these N-glycans are highly correlated to the spatial protein structure and the residential ligand binding. Interestingly, sulfation, fucosylation and bisecting N-acetylglucosamine of N-glycans were also reliably identified at the specific glycosylation sites of the two influenza proteins that may serve a crucial role in regulating the protein structure and increasing the protein abundance of the influenza virus reassortants.

INSTRUMENT(S): LTQ FT

ORGANISM(S): Homo Sapiens (human)

DISEASE(S): Influenza

SUBMITTER: Yi-Min She

LAB HEAD: Terry Cyr

PROVIDER: PXD007037 | Pride | 2018-11-21

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	10_LTQ_FT_20120224_05_X181A_AspN_narrowrangescan_65min.RAW	Raw
	10_LTQ_FT_20120224_06_X181A_AspN_narrowrangescan_500_1000.RAW	Raw
	10_LTQ_FT_20120224_07_X181A_AspN_narrowrangescan_1000_1600.RAW	Raw
	11_LTQ_FT_20111027_07_121xp_ProteinaseK_65minrun.RAW	Raw
	12_LTQ_FT_20111027_13_181A_ProteinaseK_65minrun.RAW	Raw

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Topological N-glycosylation and site-specific N-glycan sulfation of influenza proteins in the highly expressed H1N1 candidate vaccines.

She Yi-Min YM Farnsworth Aaron A Li Xuguang X Cyr Terry D TD

Scientific reports 20170831 1

The outbreak of a pandemic influenza H1N1 in 2009 required the rapid generation of high-yielding vaccines against the A/California/7/2009 virus, which were achieved by either addition or deletion of a glycosylation site in the influenza proteins hemagglutinin and neuraminidase. In this report, we have systematically evaluated the glycan composition, structural distribution and topology of glycosylation for two high-yield candidate reassortant vaccines (NIBRG-121xp and NYMC-X181A) by combining va ...[more]

PMID: 28860626

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