Virion Structure of Iflavirus Slow Bee Paralysis Virus at
2.6-Angstrom Resolution

J 2016

Virion Structure of Iflavirus Slow Bee Paralysis Virus at 2.6-Angstrom Resolution

KALYNYCH, Sergei; Antonin PRIDAL; Lenka PÁLKOVÁ; Yevgen LEVDANSKY; Joachim R. DE MIRANDA et al.

Základní údaje

Originální název

Virion Structure of Iflavirus Slow Bee Paralysis Virus at 2.6-Angstrom Resolution

Autoři

KALYNYCH, Sergei; Antonin PRIDAL; Lenka PÁLKOVÁ; Yevgen LEVDANSKY; Joachim R. DE MIRANDA a Pavel PLEVKA

Vydání

JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2016, 0022-538X

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10600 1.6 Biological sciences

Stát vydavatele

Spojené státy

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 4.663

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14740/16:00093718

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

COLONY COLLAPSE DISORDER; PICORNA-LIKE-VIRUS; APIS-MELLIFERA L.; DEFORMED WING VIRUS; HUMAN RHINOVIRUS 16; HONEY-BEE; CRYSTAL-STRUCTURE; CRYSTALLOGRAPHIC STRUCTURE; VARROA-DESTRUCTOR; ELECTRON-DENSITY

Štítky

rivok

Změněno: 23. 3. 2017 10:52, Mgr. Eva Špillingová

Anotace

V originále

The western honeybee (Apis mellifera) is the most important commercial insect pollinator. However, bees are under pressure from habitat loss, environmental stress, and pathogens, including viruses that can cause lethal epidemics. Slow bee paralysis virus (SBPV) belongs to the Iflaviridae family of nonenveloped single-stranded RNA viruses. Here we present the structure of the SBPV virion determined from two crystal forms to resolutions of 3.4 angstrom and 2.6 angstrom. The overall structure of the virion resembles that of picornaviruses, with the three major capsid proteins VP1 to 3 organized into a pseudo-T3 icosahedral capsid. However, the SBPV capsid protein VP3 contains a C-terminal globular domain that has not been observed in other viruses from the order Picornavirales. The protruding (P) domains form "crowns" on the virion surface around each 5-fold axis in one of the crystal forms. However, the P domains are shifted 36 angstrom toward the 3-fold axis in the other crystal form. Furthermore, the P domain contains the Ser-His-Asp triad within a surface patch of eight conserved residues that constitutes a putative catalytic or receptor-binding site. The movements of the domain might be required for efficient substrate cleavage or receptor binding during virus cell entry. In addition, capsid protein VP2 contains an RGD sequence that is exposed on the virion surface, indicating that integrins might be cellular receptors of SBPV. IMPORTANCE Pollination by honeybees is needed to sustain agricultural productivity as well as the biodiversity of wild flora. However, honey-bee populations in Europe and North America have been declining since the 1950s. Honeybee viruses from the Iflaviridae family are among the major causes of honeybee colony mortality. We determined the virion structure of an Iflavirus, slow bee paralysis virus (SBPV). SBPV exhibits unique structural features not observed in other picorna-like viruses. The SBPV capsid protein VP3 has a large C-terminal domain, five of which form highly prominent protruding "crowns" on the virion surface. However, the domains can change their positions depending on the conditions of the environment. The domain includes a putative catalytic or receptor binding site that might be important for SBPV cell entry.

Citovat

KALYNYCH, Sergei; Antonin PRIDAL; Lenka PÁLKOVÁ; Yevgen LEVDANSKY; Joachim R. DE MIRANDA a Pavel PLEVKA. Virion Structure of Iflavirus Slow Bee Paralysis Virus at 2.6-Angstrom Resolution. JOURNAL OF VIROLOGY. WASHINGTON: AMER SOC MICROBIOLOGY, 2016, roč. 90, č. 16, s. 7444-7455. ISSN 0022-538X. Dostupné z: https://doi.org/10.1128/JVI.00680-16.

@article{1373970,
   author = {Kalynych, Sergei and Pridal, Antonin and Pálková, Lenka and Levdansky, Yevgen and de Miranda, Joachim R. and Plevka, Pavel},
   article_location = {WASHINGTON},
   article_number = {16},
   doi = {https://doi.org/10.1128/JVI.00680-16},
   keywords = {COLONY COLLAPSE DISORDER; PICORNA-LIKE-VIRUS; APIS-MELLIFERA L.; DEFORMED WING VIRUS; HUMAN RHINOVIRUS 16; HONEY-BEE; CRYSTAL-STRUCTURE; CRYSTALLOGRAPHIC STRUCTURE; VARROA-DESTRUCTOR; ELECTRON-DENSITY},
   language = {eng},
   issn = {0022-538X},
   journal = {JOURNAL OF VIROLOGY},
   title = {Virion Structure of Iflavirus Slow Bee Paralysis Virus at 2.6-Angstrom Resolution},
   url = {http://jvi.asm.org/content/90/16/7444},
   volume = {90},
   year = {2016}
}

TY  - JOUR
ID  - 1373970
AU  - Kalynych, Sergei - Pridal, Antonin - Pálková, Lenka - Levdansky, Yevgen - de Miranda, Joachim R. - Plevka, Pavel
PY  - 2016
TI  - Virion Structure of Iflavirus Slow Bee Paralysis Virus at 2.6-Angstrom Resolution
JF  - JOURNAL OF VIROLOGY
VL  - 90
IS  - 16
SP  - 7444-7455
EP  - 7444-7455
PB  - AMER SOC MICROBIOLOGY
SN  - 0022538X
KW  - COLONY COLLAPSE DISORDER
KW  - PICORNA-LIKE-VIRUS
KW  - APIS-MELLIFERA L.
KW  - DEFORMED WING VIRUS
KW  - HUMAN RHINOVIRUS 16
KW  - HONEY-BEE
KW  - CRYSTAL-STRUCTURE
KW  - CRYSTALLOGRAPHIC STRUCTURE
KW  - VARROA-DESTRUCTOR
KW  - ELECTRON-DENSITY
UR  - http://jvi.asm.org/content/90/16/7444
L2  - http://jvi.asm.org/content/90/16/7444
N2  - The western honeybee (Apis mellifera) is the most important commercial insect pollinator. However, bees are under pressure from habitat loss, environmental stress, and pathogens, including viruses that can cause lethal epidemics. Slow bee paralysis virus (SBPV) belongs to the Iflaviridae family of nonenveloped single-stranded RNA viruses. Here we present the structure of the SBPV virion determined from two crystal forms to resolutions of 3.4 angstrom and 2.6 angstrom. The overall structure of the virion resembles that of picornaviruses, with the three major capsid proteins VP1 to 3 organized into a pseudo-T3 icosahedral capsid. However, the SBPV capsid protein VP3 contains a C-terminal globular domain that has not been observed in other viruses from the order Picornavirales. The protruding (P) domains form "crowns" on the virion surface around each 5-fold axis in one of the crystal forms. However, the P domains are shifted 36 angstrom toward the 3-fold axis in the other crystal form. Furthermore, the P domain contains the Ser-His-Asp triad within a surface patch of eight conserved residues that constitutes a putative catalytic or receptor-binding site. The movements of the domain might be required for efficient substrate cleavage or receptor binding during virus cell entry. In addition, capsid protein VP2 contains an RGD sequence that is exposed on the virion surface, indicating that integrins might be cellular receptors of SBPV. IMPORTANCE Pollination by honeybees is needed to sustain agricultural productivity as well as the biodiversity of wild flora. However, honey-bee populations in Europe and North America have been declining since the 1950s. Honeybee viruses from the Iflaviridae family are among the major causes of honeybee colony mortality. We determined the virion structure of an Iflavirus, slow bee paralysis virus (SBPV). SBPV exhibits unique structural features not observed in other picorna-like viruses. The SBPV capsid protein VP3 has a large C-terminal domain, five of which form highly prominent protruding "crowns" on the virion surface. However, the domains can change their positions depending on the conditions of the environment. The domain includes a putative catalytic or receptor binding site that might be important for SBPV cell entry.
ER  -

KALYNYCH, Sergei; Antonin PRIDAL; Lenka PÁLKOVÁ; Yevgen LEVDANSKY; Joachim R. DE MIRANDA a Pavel PLEVKA. Virion Structure of Iflavirus Slow Bee Paralysis Virus at 2.6-Angstrom Resolution. \textit{JOURNAL OF VIROLOGY}. WASHINGTON: AMER SOC MICROBIOLOGY, 2016, roč.~90, č.~16, s.~7444-7455. ISSN~0022-538X. Dostupné z: https://doi.org/10.1128/JVI.00680-16.

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