J 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

DOI

UT WoS

000573234700005

Klíčová slova anglicky

Glycobiology; Virology

Štítky

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
Název: MSCAfellow@MUNI
GA17-02196S, projekt VaV
Název: Strukturní studie flavivirů a mechanismu jejich neutralizace protilátkami
Investor: Grantová agentura ČR, Strukturní studie flavivirů a mechanismu jejich neutralizace protilátkami
90127, velká výzkumná infrastruktura
Název: CIISB II