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  Site-specific glycosylation of SARS-CoV-2: Big challenges in mass spectrometry analysis

Campos, D., Girgis, M., & Sanda, M. (2022). Site-specific glycosylation of SARS-CoV-2: Big challenges in mass spectrometry analysis. PROTEOMICS, e2100322. doi:10.1002/pmic.202100322.

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 Creators:
Campos, Diana1, Author           
Girgis, Michael, Author
Sanda, Miloslav1, Author           
Affiliations:
1Biomolecular Mass Spectrometry, Max Planck Institute for Heart and Lung Research, Max Planck Society, ou_2591705              

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 Abstract: Glycosylation of viral proteins is required for the progeny formation and infectivity of virtually all viruses. It is increasingly clear that distinct glycans also play pivotal roles in the virus's ability to shield and evade the host's immune system. Recently, there has been a great advancement in structural identification and quantitation of viral glycosylation, especially spike proteins. Given the ongoing pandemic and the high demand for structure analysis of SARS-CoV-2 densely glycosylated spike protein, mass spectrometry methodologies have been employed to accurately determine glycosylation patterns. There are still many challenges in the determination of site-specific glycosylation of SARS-CoV-2 viral spike protein. This is compounded by some conflicting results regarding glycan site occupancy and glycan structural characterization. These are probably due to differences in the expression systems, form of expressed spike glycoprotein, MS methodologies, and analysis software. In this review, we recap the glycosylation of spike protein and compare among various studies. Also, we describe the most recent advancements in glycosylation analysis in greater detail and we explain some misinterpretation of previously observed data in recent publications. Our study provides a comprehensive view of the spike protein glycosylation and highlights the importance of consistent glycosylation determination.

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 Dates: 2022-06-14
 Publication Status: Published online
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 Rev. Type: -
 Identifiers: ISI: 000814401600001
DOI: 10.1002/pmic.202100322
PMID: 35700310
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Title: PROTEOMICS
Source Genre: Journal
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Pages: - Volume / Issue: - Sequence Number: e2100322 Start / End Page: - Identifier: ISSN: 1615-9853