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Comprehensive N-glycosylation mapping of envelope glycoprotein from tick-borne encephalitis virus grown in human and tick cells

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60077344%3A_____%2F20%3A00538602" target="_blank" >RIV/60077344:_____/20:00538602 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216224:14740/20:00114734 RIV/00027162:_____/20:N0000107

  • Result on the web

    <a href="https://www.nature.com/articles/s41598-020-70082-2" target="_blank" >https://www.nature.com/articles/s41598-020-70082-2</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.1038/s41598-020-70082-2" target="_blank" >10.1038/s41598-020-70082-2</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

    Comprehensive N-glycosylation mapping of envelope glycoprotein from tick-borne encephalitis virus grown in human and tick cells

  • Original language description

    Tick-borne encephalitis virus (TBEV) is the causative agent of severe human neuroinfections that most commonly occur after a tick bite. N-Glycosylation of the TBEV envelope (E) glycoprotein is critical for virus egress in mammalian cells, but not in tick cells. In addition, glycans have been reported to mask specific antigenic sites from recognition by neutralizing antibodies. In this regard, the main purpose of our study was to investigate the profile of N-glycans linked to the E protein of TBEV when grown in human neuronal cells and compare it to the profile of virus grown in tick cells. Mass spectrometric analysis revealed significant differences in these profiles. High-mannose glycan with five mannose residues (Man(5)GlcNAc(2)), a complex biantennary galactosylated structure with core fucose (Gal(2)GlcNAc(2)Man(3)GlcNAc(2)Fuc), and a group of hybrid glycans with the composition Gal(0-1)GlcNAc(1)Man(3-5)GlcNAc(2)Fuc(0-1) were confirmed as the main asparagine-linked oligosaccharides on the surface of TBEV derived from human neuronal cells. The observed pattern was supported by examination of the glycopeptides, providing additional information about the glycosylation site in the E protein. In contrast, the profile of TBEV grown in tick cells showed that paucimannose (Man(3-4)GlcNAc(2)Fuc(0-1)) and high-mannose structures with five and six mannoses (Man(5-6)GlcNAc(2)) were major glycans on the viral surface. The reported results complement existing crystallography and cryoelectron tomography data on the E protein structure and could be instrumental for designing carbohydrate-binding antiviral agents active against TBEV.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

    Result was created during the realization of more than one project. More information in the Projects tab.

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2020

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    Scientific Reports

  • ISSN

    2045-2322

  • e-ISSN

  • Volume of the periodical

    10

  • Issue of the periodical within the volume

    1

  • Country of publishing house

    GB - UNITED KINGDOM

  • Number of pages

    10

  • Pages from-to

    13204

  • UT code for WoS article

    000573234700005

  • EID of the result in the Scopus database

    2-s2.0-85089155594