J 2017

Virion Structure of Black Queen Cell Virus, a Common Honeybee Pathogen

SPURNÝ, Radovan, Antonin PRIDAL, Lenka PÁLKOVÁ, Hoa Khanh TRAN KIEM, Joachim R. DE MIRANDA et. al.

Základní údaje

Originální název

Virion Structure of Black Queen Cell Virus, a Common Honeybee Pathogen

Autoři

SPURNÝ, Radovan (703 Slovensko, domácí), Antonin PRIDAL (203 Česká republika), Lenka PÁLKOVÁ (203 Česká republika, domácí), Hoa Khanh TRAN KIEM (704 Vietnam, domácí), Joachim R. DE MIRANDA (752 Švédsko) a Pavel PLEVKA (203 Česká republika, garant, domácí)

Vydání

JOURNAL OF VIROLOGY, WASHINGTON, AMER SOC MICROBIOLOGY, 2017, 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

Impakt faktor

Impact factor: 4.368

Kód RIV

RIV/00216224:14740/17:00096847

Organizační jednotka

Středoevropský technologický institut

UT WoS

000398098300016

Klíčová slova anglicky

virus; Apis mellifera; honey bee; honeybee; Picornavirales; Dicistroviridae; Cripavirus; Triatovirus; virion; structure; X ray; crystallography; capsid; insect disease; X-ray crystallography

Štítky

Příznaky

Mezinárodní význam, Recenzováno
Změněno: 27. 2. 2018 16:54, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

Viral diseases are a major threat to honeybee (Apis mellifera) populations worldwide and therefore an important factor in reliable crop pollination and food security. Black queen cell virus (BQCV) is the etiological agent of a fatal disease of honeybee queen larvae and pupae. The virus belongs to the genus Triatovirus from the family Dicistroviridae, which is part of the order Picornavirales. Here we present a crystal structure of BQCV determined to a resolution of 3.4 angstrom. The virion is formed by 60 copies of each of the major capsid proteins VP1, VP2, and VP3; however, there is no density corresponding to a 75-residue-long minor capsid protein VP4 encoded by the BQCV genome. We show that the VP4 subunits are present in the crystallized virions that are infectious. This aspect of the BQCV virion is similar to that of the previously characterized triatoma virus and supports the recent establishment of the separate genus Triatovirus within the family Dicistroviridae. The C terminus of VP1 and CD loops of capsid proteins VP1 and VP3 of BQCV form 34-angstrom-tall finger-like protrusions at the virion surface. The protrusions are larger than those of related dicistroviruses. IMPORTANCE The western honeybee is the most important pollinator of all, and it is required to sustain the agricultural production and biodiversity of wild flowering plants. However, honeybee populations worldwide are suffering from virus infections that cause colony losses. One of the most common, and least known, honeybee pathogens is black queen cell virus (BQCV), which at high titers causes queen larvae and pupae to turn black and die. Here we present the three-dimensional virion structure of BQCV, determined by X-ray crystallography. The structure of BQCV reveals large protrusions on the virion surface. Capsid protein VP1 of BQCV does not contain a hydrophobic pocket. Therefore, the BQCV virion structure provides evidence that capsid-binding antiviral compounds that can prevent the replication of vertebrate picornaviruses may be ineffective against honeybee virus infections.

Návaznosti

LM2010005, projekt VaV
Název: Velká infrastruktura CESNET (Akronym: VI CESNET)
Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Velká infrastruktura CESNET
LM2015043, projekt VaV
Název: Česká infrastruktura pro integrativní strukturní biologii (Akronym: CIISB)
Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Czech Infrastructure for Integrative Structural Biology
LQ1601, projekt VaV
Název: CEITEC 2020 (Akronym: CEITEC2020)
Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, CEITEC 2020