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    Home > Active Ingredient News > Infection > Cell Res: Breakthrough!

    Cell Res: Breakthrough!

    • Last Update: 2021-08-13
    • Source: Internet
    • Author: User
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    Protein glycosylation modification is one of the most important post-translational modifications in organisms, occurring on 50%-70% of the protein in the cell
    .


    The glycosylation modification of viral envelope protein has a wide range of functions, including regulating protein stability, virus tropism, and protecting potential epitopes from immune surveillance


    Recently, the Huang Chaolan team of the Precision Medicine Multi-omics Research Center of Peking University Health Science Center, the Gao Fu team of the Chinese Academy of Sciences, and the peak team of the Tianjin Institute of Industrial Biotechnology of the Chinese Academy of Sciences have carried out collaborative research, using mass spectrometry-based glycosylation identification technology, revealing for the first time The O-glycosylation modification map of the S protein extracted from the virus particles is presented, and the O-Follow-N O-glycosylation modification rule is proposed
    .


    The research titled " O-glycosylation pattern of the SARS-CoV-2 spike protein reveals an "O-Follow-N" rule " was published online in Cell Research on August 2, 2021


    O-glycosylation pattern of the SARS-CoV-2 spike protein reveals an “O-Follow-N” rule

    In order to obtain a complete map of the N- and O-glycosylation modification of S protein in its natural state, the researchers obtained S protein from SARS-CoV-2 virus particles and used a variety of proteases to digest it into peptides, using nanoliter liquid Chromatography and the ultra-high-resolution Orbitrap Eclipse Tribrid three-in-one mass spectrometer, using stepped collisional energy SCE (stepped collisional energy SCE), HCD (Higher-energy collisional dissociation) and HCDpdEThcD three fragmentation methods for mass spectrometry analysis
    .

    In this study, the researchers not only successfully identified 22 previously reported N-glycosylation sites, but also for the first time identified 17 O-glycosylation sites on the S protein extracted from SARS-CoV-2 virus particles.
    Modification site
    .


    It is worth noting that the researchers found that among these 17 sites, 11 sites are located near the glycosylated asparagine (Asn)


    Figure.
    The glycosylation modification of SARS-CoV-2 virus S protein follows the "O-Follow-N" rule

    Figure.
    The glycosylation modification of the SARS-CoV-2 virus S protein follows the "O-Follow-N" rule .
    The graph.
    The glycosylation modification of the SARS-CoV-2 virus S protein follows the "O-Follow-N" rule

    Based on cutting-edge mass spectrometry identification technology, this study revealed the O-glycosylation modification spectrum of S protein, and proposed the "O-Follow-N" rule of O-glycosylation modification.
    This rule may be applicable to other proteins, suggesting O- Glycosylation modification has potential new mechanisms, especially the possible synergy between N- and O-glycosylation modification, which is expected to greatly promote research in the field of glycobiology in the future
    .

    Previously, the multi-omics center team led by Director Huang Chaolan also worked closely with the multi-disciplinary team led by Academician Gao Fu, revealing that patients with early COVID-19 infection have significant immunosuppression, and for the first time proposed that the pathogenesis of COVID-19 may have "two problems".
    Phase" mode 3
    .


    Under the leadership of Professor Huang Chaolan, the Multi-omics Center will continue to deepen the development of cutting-edge technology and methods based on the in-depth cross-integration of clinical, cutting-edge technology and basic disciplines, and provide the most quality-guaranteed protein for the promotion of innovative research in basic biology and clinical fields.


    Gao Fu, Academician of the Institute of Microbiology, Chinese Academy of Sciences, Professor Huang Chaolan, Director of the Precision Medicine Multi-omics Research Center of Peking University Health Science Center, Chen Yang, Associate Researcher of the Precision Medicine Multi-omics Research Center of Peking University Health Science Center, and Professor Gao Feng, Tianjin Institute of Industrial Biotechnology, Chinese Academy of Sciences Co-corresponding author; Dr.


    Original source:

    Original source:

    Tian, ​​W.


    O-glycosylation pattern of the SARS- CoV-2 spike protein reveals an "O-Follow-N" rule in this message
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