PRIDE Assigned Tags:Biomedical Dataset
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Influenza A virus- integrated glycomics, proteomics and glycoproteomics
This study describes how site-specific glycosylation of Influenza A virus changes in response to pressures from the host immune system, thereby allowing the virus to evolve and escape neutralization. We compared the glycosylation patterns of different virus strains as they evolve and correlated this information with changes in biological activity. Furthermore, modelling and molecular dynamics studies were performed to understand the basis for glycan microheterogeneity and interactions of the virions with host-immune molecules.
Sample Processing Protocol
All samples were subjected to proteomics, glycomics and glycoprotemics experiments. Virus samples were deglycosylated and subjected to C18 LC-MS/MS for proteomics. Released glycans were subjected to HILIC-MS for glycomics. intact glycopeptides were analyzed by online HILIC enrichment and C18 LC-MS/MS.
Data Processing Protocol
Proteomics data were analyzed using PEAKS for error-tolerant database and de novo proteomics searches. Glycomics and glycoproteomics data were analyzed using an in-house data analysis pipeline, GlycReSoft.
Kshitij Khatri, Boston University
Joseph Zaia, Center for Biomedical Mass Spectrometry, Department of Biochemistry, Boston University School of Medicine, Boston, MA 02118, United States of America ( lab head )
Khatri K, Klein JA, White MR, Grant OC, Leymarie N, Woods RJ, Hartshorn KL, Zaia J. Integrated omics and computational glycobiology reveal structural basis for Influenza A virus glycan microheterogeneity and host interactions. Mol Cell Proteomics. 2016 Mar 16. pii: mcp.M116.058016 PubMed: 26984886