Dataset Information

Intact mass LC-MS analysis of Flu B HA1 and HA2 proteins

ABSTRACT: To determine the sequences of the Flu HA1 and HA2 proteins, we performed intact mass LC-MS analysis. By reducing disulfide bridges two peaks corresponding to the HA1 and HA2 components were detected. Mass profiles were obtained for both glycosylated and deglycosylated HA proteins.

INSTRUMENT(S):

ORGANISM(S): Influenza A Virus (a/aquatic Bird/hong Kong/m603/98(h11n1))

TISSUE(S): Organism Or Virus Or Viroid

DISEASE(S): Influenza

SUBMITTER: Sem Tamara

LAB HEAD: Johannes P.M. Langedijk

PROVIDER: PXD046130 | Pride | 2025-05-06

REPOSITORIES: Pride

ACCESS DATA

Dataset's files

Source:

			Action	DRS
	Mass_table.xlsx	Xlsx
	UFV221176_Pool2_PNF_TCEP_200ng_LockSpray_noCE_01.raw.zip	Raw
	UFV221176_Pool2_TCEP_200ng_LockSpray_noCE_01.raw.zip	Raw
	checksum.txt	Txt

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Publications

Engineering a cleaved, prefusion-stabilized influenza B virus hemagglutinin by identification and locking of all six pH switches.

Juraszek Jarek J Milder Fin J FJ Yu Xiaodi X Blokland Sven S van Overveld Daan D Abeywickrema Pravien P Tamara Sem S Sharma Sujata S Rutten Lucy L Bakkers Mark J G MJG Langedijk Johannes P M JPM

PNAS nexus 20241011 10

Vaccine components based on viral fusion proteins require high stability of the native prefusion conformation for optimal potency and manufacturability. In the case of influenza B virus hemagglutinin (HA), the stem's conformation relies on efficient cleavage. In this study, we identified six pH-sensitive regions distributed across the entire ectodomain where protonated histidines assume either a repulsive or an attractive role. Substitutions in these areas enhanced the protein's expression, qual ...[more]

PMID: 39445049

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