2020
Comprehensive N-glycosylation mapping of envelope glycoprotein from tick-borne encephalitis virus grown in human and tick cells
LATTOVÁ, Erika, Petra STRAKOVA, Petra POKORNA-FORMANOVA, Libor GRUBHOFFER, Lesley BELL-SAKYI et. al.Základní údaje
Originální název
Comprehensive N-glycosylation mapping of envelope glycoprotein from tick-borne encephalitis virus grown in human and tick cells
Autoři
LATTOVÁ, Erika (703 Slovensko, garant, domácí), Petra STRAKOVA, Petra POKORNA-FORMANOVA, Libor GRUBHOFFER, Lesley BELL-SAKYI, Zbyněk ZDRÁHAL (203 Česká republika, domácí), Martin PALUS a Daniel RUZEK
Vydání
Scientific Reports, Berlin, Nature Research, 2020, 2045-2322
Další údaje
Jazyk
angličtina
Typ výsledku
Článek v odborném periodiku
Obor
10608 Biochemistry and molecular biology
Stát vydavatele
Německo
Utajení
není předmětem státního či obchodního tajemství
Odkazy
Impakt faktor
Impact factor: 4.379
Kód RIV
RIV/00216224:14740/20:00114734
Organizační jednotka
Středoevropský technologický institut
UT WoS
000573234700005
Klíčová slova anglicky
Glycobiology; Virology
Příznaky
Mezinárodní význam, Recenzováno
Změněno: 2. 11. 2024 20:28, Ing. Martina Blahová
Anotace
V originále
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.
Návaznosti
EF17_050/0008496, projekt VaV |
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GA17-02196S, projekt VaV |
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90127, velká výzkumná infrastruktura |
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