J 2017

Cryo-electron Microscopy Study of the Genome Release of the Dicistrovirus Israeli Acute Bee Paralysis Virus

MULLAPUDI, Edukondalu, Tibor FÜZIK, Antonin PRIDAL a Pavel PLEVKA

Základní údaje

Originální název

Cryo-electron Microscopy Study of the Genome Release of the Dicistrovirus Israeli Acute Bee Paralysis Virus

Autoři

MULLAPUDI, Edukondalu (356 Indie, domácí), Tibor FÜZIK (703 Slovensko, domácí), Antonin PRIDAL (203 Česká republika) 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/00216224:14740/17:00096372

Organizační jednotka

Středoevropský technologický institut

DOI

UT WoS

000393883300022

Klíčová slova anglicky

virus; Apis mellifera; honey bee; honeybee; Picornavirales; Dicistroviridae; Aparavirus; virion; structure; cryo; electron microscopy; capsid; genome; release; uncoating; colony collapse disorder; CCD; empty

Štítky

Příznaky

Mezinárodní význam, Recenzováno
Změněno: 23. 2. 2018 13:18, Mgr. Pavla Foltynová, Ph.D.

Anotace

V originále

Viruses of the family Dicistroviridae can cause substantial economic damage by infecting agriculturally important insects. Israeli acute bee paralysis virus (IAPV) causes honeybee colony collapse disorder in the United States. High-resolution molecular details of the genome delivery mechanism of dicistroviruses are unknown. Here we present a cryo-electron microscopy analysis of IAPV virions induced to release their genomes in vitro. We determined structures of full IAPV virions primed to release their genomes to a resolution of 3.3 angstrom and of empty capsids to a resolution of 3.9 angstrom. We show that IAPV does not form expanded A particles before genome release as in the case of related enteroviruses of the family Picornaviridae. The structural changes observed in the empty IAPV particles include detachment of the VP4 minor capsid proteins from the inner face of the capsid and partial loss of the structure of the N-terminal arms of the VP2 capsid proteins. Unlike the case for many picornaviruses, the empty particles of IAPV are not expanded relative to the native virions and do not contain pores in their capsids that might serve as channels for genome release. Therefore, rearrangement of a unique region of the capsid is probably required for IAPV genome release. IMPORTANCE Honeybee populations in Europe and North America are declining due to pressure from pathogens, including viruses. Israeli acute bee paralysis virus (IAPV), a member of the family Dicistroviridae, causes honeybee colony collapse disorder in the United States. The delivery of virus genomes into host cells is necessary for the initiation of infection. Here we present a structural cryo-electron microscopy analysis of IAPV particles induced to release their genomes. We show that genome release is not preceded by an expansion of IAPV virions as in the case of related picornaviruses that infect vertebrates. Furthermore, minor capsid proteins detach from the capsid upon genome release. The genome leaves behind empty particles that have compact protein shells.

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