{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"submitter":["Miller RM"],"funding":["Biomedical Laboratory Research and Development, VA Office of Research and Development","Sanofi"],"pubmed_abstract":["<h4>Rationale</h4>We report the N-glycosylation pattern of a Sf9 insect cell derived recombinant spike proteins being developed as candidate vaccine antigens for SARS-CoV-2 (COVID-19) (Sanofi). The method has been optimised to produce peptides with single, isolated glycosylation sites using multiple protease digests. The development and use of glycopeptide libraries from previous developmental phases allowed for faster analysis than processing data sets from individual batches from first principles.<h4>Method</h4>Purified spike proteins were reduced, alkylated, and digested with proteolytic enzymes. Three different protease digests were utilised to generate peptides with isolated glycosylation sites. The glycopeptides were then analysed using a Waters Q-TOF while using a data dependent acq"],"journal":["Rapid communications in mass spectrometry : RCM"],"pagination":["e9452"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9877958"],"repository":["biostudies-literature"],"pubmed_title":["Glycopeptide Characterization of Sf9-Derived SARS-CoV-2 Spike Protein Recombinant Vaccine Candidates Expedited by the Use of Glycopeptide Libraries."],"pmcid":["PMC9877958"],"funding_grant_id":["HHSO100201600005I"],"pubmed_authors":["Miller RM","Perkins GL","Bush D","DeGraan-Weber N","Tartiere A"],"additional_accession":[]},"is_claimable":false,"name":"Glycopeptide Characterization of Sf9-Derived SARS-CoV-2 Spike Protein Recombinant Vaccine Candidates Expedited by the Use of Glycopeptide Libraries.","description":"<h4>Rationale</h4>We report the N-glycosylation pattern of a Sf9 insect cell derived recombinant spike proteins being developed as candidate vaccine antigens for SARS-CoV-2 (COVID-19) (Sanofi). The method has been optimised to produce peptides with single, isolated glycosylation sites using multiple protease digests. The development and use of glycopeptide libraries from previous developmental phases allowed for faster analysis than processing data sets from individual batches from first principles.<h4>Method</h4>Purified spike proteins were reduced, alkylated, and digested with proteolytic enzymes. Three different protease digests were utilised to generate peptides with isolated glycosylation sites. The glycopeptides were then analysed using a Waters Q-TOF while using a data dependent acq","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Dec","modification":"2025-04-25T20:10:37.425Z","creation":"2025-04-06T08:18:34.829Z"},"accession":"S-EPMC9877958","cross_references":{"pubmed":["36478308"],"doi":["10.1002/rcm.9452"]}}