Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody

Tick-borne encephalitis virus (TBEV) causes 13,000 cases of human meningitis and encephalitis annually. However, the structure of the TBEV virion and its interactions with antibodies are unknown. Here, we present cryo-EM structures of the native TBEV virion and its complex with Fab fragments of neut...

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Published inNature communications Vol. 9; no. 1; pp. 436 - 11
Main Authors Füzik, Tibor, Formanová, Petra, Růžek, Daniel, Yoshii, Kentaro, Niedrig, Matthias, Plevka, Pavel
Format Journal Article
LanguageEnglish
Published London Nature Publishing Group UK 30.01.2018
Nature Publishing Group
Nature Portfolio
Subjects
101/1
101/28
13/106
631/326/596/2148
631/326/596/2557
631/535/1258/1259
Antibodies, Neutralizing - biosynthesis
Antibodies, Neutralizing - chemistry
Antibodies, Viral - biosynthesis
Antibodies, Viral - chemistry
Cell Line, Tumor
Cryoelectron Microscopy
Detachment
Encephalitis
Encephalitis Viruses, Tick-Borne - genetics
Encephalitis Viruses, Tick-Borne - metabolism
Encephalitis Viruses, Tick-Borne - ultrastructure
Fab
Fragmentation
Fragments
Gene Expression
Genomes
Glycoproteins
Histidine
Humanities and Social Sciences
Humans
Hydrogen-Ion Concentration
Immunoglobulin Fab Fragments - biosynthesis
Immunoglobulin Fab Fragments - chemistry
Membrane fusion
Membrane Fusion - genetics
Membrane proteins
Membranes
Meningitis
Monoclonal antibodies
multidisciplinary
Neurons - pathology
Neurons - virology
Neutralization
Neutralizing
pH effects
Protein Domains
Protein Multimerization
Proteins
Science
Science (multidisciplinary)
Tick-borne encephalitis
Viral envelope proteins
Viral Proteins - chemistry
Viral Proteins - genetics
Viral Proteins - metabolism
Virion - genetics
Virion - metabolism
Virion - ultrastructure
Virions
Virus Internalization
Viruses
Online AccessGet full text

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Abstract Tick-borne encephalitis virus (TBEV) causes 13,000 cases of human meningitis and encephalitis annually. However, the structure of the TBEV virion and its interactions with antibodies are unknown. Here, we present cryo-EM structures of the native TBEV virion and its complex with Fab fragments of neutralizing antibody 19/1786. Flavivirus genome delivery depends on membrane fusion that is triggered at low pH. The virion structure indicates that the repulsive interactions of histidine side chains, which become protonated at low pH, may contribute to the disruption of heterotetramers of the TBEV envelope and membrane proteins and induce detachment of the envelope protein ectodomains from the virus membrane. The Fab fragments bind to 120 out of the 180 envelope glycoproteins of the TBEV virion. Unlike most of the previously studied flavivirus-neutralizing antibodies, the Fab fragments do not lock the E-proteins in the native-like arrangement, but interfere with the process of virus-induced membrane fusion. The tick-borne encephalitis virus (TBEV) causes thousands of cases of meningitis and encephalitis annually. Here, the authors describe a cryo-EM structure of the TBEV virion bound by Fab fragments of the neutralizing antibody 19/1786, revealing a mechanism whereby this antibody prevents virus membrane fusion.
AbstractList Tick-borne encephalitis virus (TBEV) causes 13,000 cases of human meningitis and encephalitis annually. However, the structure of the TBEV virion and its interactions with antibodies are unknown. Here, we present cryo-EM structures of the native TBEV virion and its complex with Fab fragments of neutralizing antibody 19/1786. Flavivirus genome delivery depends on membrane fusion that is triggered at low pH. The virion structure indicates that the repulsive interactions of histidine side chains, which become protonated at low pH, may contribute to the disruption of heterotetramers of the TBEV envelope and membrane proteins and induce detachment of the envelope protein ectodomains from the virus membrane. The Fab fragments bind to 120 out of the 180 envelope glycoproteins of the TBEV virion. Unlike most of the previously studied flavivirus-neutralizing antibodies, the Fab fragments do not lock the E-proteins in the native-like arrangement, but interfere with the process of virus-induced membrane fusion.
Tick-borne encephalitis virus (TBEV) causes 13,000 cases of human meningitis and encephalitis annually. However, the structure of the TBEV virion and its interactions with antibodies are unknown. Here, we present cryo-EM structures of the native TBEV virion and its complex with Fab fragments of neutralizing antibody 19/1786. Flavivirus genome delivery depends on membrane fusion that is triggered at low pH. The virion structure indicates that the repulsive interactions of histidine side chains, which become protonated at low pH, may contribute to the disruption of heterotetramers of the TBEV envelope and membrane proteins and induce detachment of the envelope protein ectodomains from the virus membrane. The Fab fragments bind to 120 out of the 180 envelope glycoproteins of the TBEV virion. Unlike most of the previously studied flavivirus-neutralizing antibodies, the Fab fragments do not lock the E-proteins in the native-like arrangement, but interfere with the process of virus-induced membrane fusion. The tick-borne encephalitis virus (TBEV) causes thousands of cases of meningitis and encephalitis annually. Here, the authors describe a cryo-EM structure of the TBEV virion bound by Fab fragments of the neutralizing antibody 19/1786, revealing a mechanism whereby this antibody prevents virus membrane fusion.
The tick-borne encephalitis virus (TBEV) causes thousands of cases of meningitis and encephalitis annually. Here, the authors describe a cryo-EM structure of the TBEV virion bound by Fab fragments of the neutralizing antibody 19/1786, revealing a mechanism whereby this antibody prevents virus membrane fusion.
Tick-borne encephalitis virus (TBEV) causes 13,000 cases of human meningitis and encephalitis annually. However, the structure of the TBEV virion and its interactions with antibodies are unknown. Here, we present cryo-EM structures of the native TBEV virion and its complex with Fab fragments of neutralizing antibody 19/1786. Flavivirus genome delivery depends on membrane fusion that is triggered at low pH. The virion structure indicates that the repulsive interactions of histidine side chains, which become protonated at low pH, may contribute to the disruption of heterotetramers of the TBEV envelope and membrane proteins and induce detachment of the envelope protein ectodomains from the virus membrane. The Fab fragments bind to 120 out of the 180 envelope glycoproteins of the TBEV virion. Unlike most of the previously studied flavivirus-neutralizing antibodies, the Fab fragments do not lock the E-proteins in the native-like arrangement, but interfere with the process of virus-induced membrane fusion.Tick-borne encephalitis virus (TBEV) causes 13,000 cases of human meningitis and encephalitis annually. However, the structure of the TBEV virion and its interactions with antibodies are unknown. Here, we present cryo-EM structures of the native TBEV virion and its complex with Fab fragments of neutralizing antibody 19/1786. Flavivirus genome delivery depends on membrane fusion that is triggered at low pH. The virion structure indicates that the repulsive interactions of histidine side chains, which become protonated at low pH, may contribute to the disruption of heterotetramers of the TBEV envelope and membrane proteins and induce detachment of the envelope protein ectodomains from the virus membrane. The Fab fragments bind to 120 out of the 180 envelope glycoproteins of the TBEV virion. Unlike most of the previously studied flavivirus-neutralizing antibodies, the Fab fragments do not lock the E-proteins in the native-like arrangement, but interfere with the process of virus-induced membrane fusion.
ArticleNumber 436
Author Růžek, Daniel
Yoshii, Kentaro
Plevka, Pavel
Niedrig, Matthias
Füzik, Tibor
Formanová, Petra
Author_xml – sequence: 1
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  surname: Füzik
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  surname: Yoshii
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  fullname: Plevka, Pavel
  email: pavel.plevka@ceitec.muni.cz
  organization: Structural Virology, Central European Institute of Technology, Masaryk University
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Snippet Tick-borne encephalitis virus (TBEV) causes 13,000 cases of human meningitis and encephalitis annually. However, the structure of the TBEV virion and its...
The tick-borne encephalitis virus (TBEV) causes thousands of cases of meningitis and encephalitis annually. Here, the authors describe a cryo-EM structure of...
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pubmed
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StartPage 436
SubjectTerms 101/1
101/28
13/106
631/326/596/2148
631/326/596/2557
631/535/1258/1259
Antibodies, Neutralizing - biosynthesis
Antibodies, Neutralizing - chemistry
Antibodies, Viral - biosynthesis
Antibodies, Viral - chemistry
Cell Line, Tumor
Cryoelectron Microscopy
Detachment
Encephalitis
Encephalitis Viruses, Tick-Borne - genetics
Encephalitis Viruses, Tick-Borne - metabolism
Encephalitis Viruses, Tick-Borne - ultrastructure
Fab
Fragmentation
Fragments
Gene Expression
Genomes
Glycoproteins
Histidine
Humanities and Social Sciences
Humans
Hydrogen-Ion Concentration
Immunoglobulin Fab Fragments - biosynthesis
Immunoglobulin Fab Fragments - chemistry
Membrane fusion
Membrane Fusion - genetics
Membrane proteins
Membranes
Meningitis
Monoclonal antibodies
multidisciplinary
Neurons - pathology
Neurons - virology
Neutralization
Neutralizing
pH effects
Protein Domains
Protein Multimerization
Proteins
Science
Science (multidisciplinary)
Tick-borne encephalitis
Viral envelope proteins
Viral Proteins - chemistry
Viral Proteins - genetics
Viral Proteins - metabolism
Virion - genetics
Virion - metabolism
Virion - ultrastructure
Virions
Virus Internalization
Viruses
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Title Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody
URI https://link.springer.com/article/10.1038/s41467-018-02882-0
https://www.ncbi.nlm.nih.gov/pubmed/29382836
https://www.proquest.com/docview/1992655051
https://www.proquest.com/docview/1993013885
https://pubmed.ncbi.nlm.nih.gov/PMC5789857
https://doaj.org/article/9ca299bbfe594c17985845abd4f92848
Volume 9
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