LATTOVÁ, Erika, Petra STRAKOVA, Petra POKORNA-FORMANOVA, Libor GRUBHOFFER, Lesley BELL-SAKYI, Zbyněk ZDRÁHAL, Martin PALUS and Daniel RUZEK. Comprehensive N-glycosylation mapping of envelope glycoprotein from tick-borne encephalitis virus grown in human and tick cells. Scientific Reports. Berlin: Nature Research, 2020, vol. 10, No 1, p. 13204-13213. ISSN 2045-2322. Available from: https://dx.doi.org/10.1038/s41598-020-70082-2.
Other formats:   BibTeX LaTeX RIS
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
Original language English
Type of outcome Article in a journal
Field of Study 10608 Biochemistry and molecular biology
Country of publisher Germany
Confidentiality degree is not subject to a state or trade secret
WWW URL
Impact factor Impact factor: 4.379
RIV identification code RIV/00216224:14740/20:00114734
Organization unit Central European Institute of Technology
Doi http://dx.doi.org/10.1038/s41598-020-70082-2
UT WoS 000573234700005
Keywords in English Glycobiology; Virology
Tags CF PROT, rivok
Tags International impact, Reviewed
Changed by Changed by: Mgr. Pavla Foltynová, Ph.D., učo 106624. Changed: 19/3/2021 15:15.
Abstract
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 projectName: MSCAfellow@MUNI
GA17-02196S, research and development projectName: 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 projectName: Česká infrastruktura pro integrativní strukturní biologii (Acronym: CIISB)
Investor: Ministry of Education, Youth and Sports of the CR
PrintDisplayed: 27/4/2024 01:28