Detail
Článek
Článek online
FT
Medvik - BMČ
  • Je něco špatně v tomto záznamu ?

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

T. Füzik, P. Formanová, D. Růžek, K. Yoshii, M. Niedrig, P. Plevka,

. 2018 ; 9 (1) : 436. [pub] 20180130

Jazyk angličtina Země Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc18010191

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.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc18010191
003      
CZ-PrNML
005      
20230808113552.0
007      
ta
008      
180404s2018 xxk f 000 0|eng||
009      
AR
024    7_
$a 10.1038/s41467-018-02882-0 $2 doi
035    __
$a (PubMed)29382836
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a xxk
100    1_
$a Füzik, Tibor $u Structural Virology, Central European Institute of Technology, Masaryk University, Kamenice 753/5, 62500, Brno, Czech Republic.
245    10
$a Structure of tick-borne encephalitis virus and its neutralization by a monoclonal antibody / $c T. Füzik, P. Formanová, D. Růžek, K. Yoshii, M. Niedrig, P. Plevka,
520    9_
$a 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.
650    _2
$a neutralizující protilátky $x biosyntéza $x chemie $7 D057134
650    _2
$a protilátky virové $x biosyntéza $x chemie $7 D000914
650    _2
$a nádorové buněčné linie $7 D045744
650    _2
$a elektronová kryomikroskopie $7 D020285
650    _2
$a viry klíšťové encefalitidy $x genetika $x metabolismus $x ultrastruktura $7 D004669
650    _2
$a exprese genu $7 D015870
650    _2
$a lidé $7 D006801
650    _2
$a koncentrace vodíkových iontů $7 D006863
650    _2
$a imunoglobuliny - Fab fragmenty $x biosyntéza $x chemie $7 D007140
650    _2
$a fúze membrán $x genetika $7 D008561
650    _2
$a neurony $x patologie $x virologie $7 D009474
650    _2
$a proteinové domény $7 D000072417
650    _2
$a multimerizace proteinu $7 D055503
650    _2
$a virové proteiny $x chemie $x genetika $x metabolismus $7 D014764
650    _2
$a virion $x genetika $x metabolismus $x ultrastruktura $7 D014771
650    _2
$a internalizace viru $7 D053586
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Pokorná, Petra $u Department of Virology, Veterinary Research Institute, Hudcova 70, 62100, Brno, Czech Republic. $7 mzk2018988134
700    1_
$a Růžek, Daniel, $u Department of Virology, Veterinary Research Institute, Hudcova 70, 62100, Brno, Czech Republic. Institute of Parasitology, Biology Centre of the Czech Academy of Sciences, Branisovska 31, 37005, Ceske Budejovice, Czech Republic. $d 1981- $7 stk2008441707
700    1_
$a Yoshii, Kentaro $u Laboratory of Public Health, Graduate School of Veterinary Medicine, Hokkaido University, Sapporo, 060-0818, Japan.
700    1_
$a Niedrig, Matthias $u Centre for Biological Threats and Special Pathogens, Robert Koch Institute, Nordufer 20, 13353, Berlin, Germany.
700    1_
$a Plevka, Pavel $u Structural Virology, Central European Institute of Technology, Masaryk University, Kamenice 753/5, 62500, Brno, Czech Republic. pavel.plevka@ceitec.muni.cz.
773    0_
$w MED00184850 $t Nature communications $x 2041-1723 $g Roč. 9, č. 1 (2018), s. 436
856    41
$u https://pubmed.ncbi.nlm.nih.gov/29382836 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y a $z 0
990    __
$a 20180404 $b ABA008
991    __
$a 20230808113549 $b ABA008
999    __
$a ok $b bmc $g 1287676 $s 1007003
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2018 $b 9 $c 1 $d 436 $e 20180130 $i 2041-1723 $m Nature communications $n Nat Commun $x MED00184850
LZP    __
$a Pubmed-20180404

Najít záznam

Citační ukazatele

Možnosti archivace