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.

Basic information

Original name

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

Authors

LATTOVÁ, Erika (703 Slovakia, guarantor, belonging to the institution), Petra STRAKOVA, Petra POKORNA-FORMANOVA, Libor GRUBHOFFER, Lesley BELL-SAKYI, Zbyněk ZDRÁHAL (203 Czech Republic, belonging to the institution), Martin PALUS and Daniel RUZEK

Edition

Scientific Reports, Berlin, Nature Research, 2020, 2045-2322

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

Germany

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

Impact factor

Impact factor: 4.379

RIV identification code

RIV/00216224:14740/20:00114734

Organization unit

Central European Institute of Technology

DOI

UT WoS

000573234700005

Keywords in English

Glycobiology; Virology

Tags

Tags

International impact, Reviewed
Změněno: 10/10/2024 13:52, Ing. Martina Blahová

Abstract

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.

Links

EF17_050/0008496, research and development project
Name: MSCAfellow@MUNI
GA17-02196S, research and development project
Name: Strukturní studie flavivirů a mechanismu jejich neutralizace protilátkami
Investor: Czech Science Foundation, Structural studies of flaviviruses and their neutralization by antibodies
LM2018127, research and development project
Name: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)
Investor: Ministry of Education, Youth and Sports of the CR
90127, large research infrastructures
Name: CIISB II