Structures of L-BC virus and its open particle provide insight
into Totivirus capsid assembly

J 2022

Structures of L-BC virus and its open particle provide insight into Totivirus capsid assembly

GRYBCHUK, Danyil; Michaela PROCHÁZKOVÁ; Tibor FÜZIK; Aleksandras KONOVALOVAS; Saulius SERVA et al.

Základní údaje

Originální název

Structures of L-BC virus and its open particle provide insight into Totivirus capsid assembly

Autoři

GRYBCHUK, Danyil; Michaela PROCHÁZKOVÁ ; Tibor FÜZIK ; Aleksandras KONOVALOVAS; Saulius SERVA; Vyacheslav YURCHENKO a Pavel PLEVKA

Vydání

Communications Biology, Nature Research, 2022, 2399-3642

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10607 Virology

Stát vydavatele

Německo

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 5.900

Označené pro přenos do RIV

Ano

Kód RIV

RIV/00216224:14740/22:00127056

Organizační jednotka

Středoevropský technologický institut

Klíčová slova anglicky

Animals; Capsid; Capsid Proteins; Cryoelectron Microscopy; Totivirus; Viruses

Štítky

CF CRYO, CF PROT, NIVB_CEITEC, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 9. 10. 2024 13:18, Ing. Martina Blahová

Anotace

V originále

L-BC virus persists in the budding yeast Saccharomyces cerevisiae, whereas other viruses from the family Totiviridae infect a diverse group of organisms including protists, fungi, arthropods, and vertebrates. The presence of totiviruses alters the fitness of the host organisms, for example, by maintaining the killer system in yeast or increasing the virulence of Leishmania guyanensis. Despite the importance of totiviruses for their host survival, there is limited information about Totivirus structure and assembly. Here we used cryo-electron microscopy to determine the structure of L-BC virus to a resolution of 2.9 angstrom. The L-BC capsid is organized with icosahedral symmetry, with each asymmetric unit composed of two copies of the capsid protein. Decamers of capsid proteins are stabilized by domain swapping of the C-termini of subunits located around icosahedral fivefold axes. We show that capsids of 9% of particles in a purified L-BC sample were open and lacked one decamer of capsid proteins. The existence of the open particles together with domain swapping within a decamer provides evidence that Totiviridae capsids assemble from the decamers of capsid proteins. Furthermore, the open particles may be assembly intermediates that are prepared for the incorporation of the virus (+) strand RNA. A 2.9 angstrom resolution structure of the L-BC virus provides insight into the contacts between capsid proteins and the mechanism of capsid assembly.

Návaznosti

GX19-25982X, projekt VaV

Název: Analýza replikace enterovirů s využitím elektronové mikroskopie

Investor: Grantová agentura ČR, Structural study of enterovirus replication in situ

LM2018140, projekt VaV

Název: e-Infrastruktura CZ (Akronym: e-INFRA CZ)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, e-Infrastruktura CZ

LX22NPO5103, projekt VaV

Název: Národní institut virologie a bakteriologie (Akronym: NIVB)

Investor: Ministerstvo školství, mládeže a tělovýchovy ČR, Národní institut virologie a bakteriologie, 5.1 EXCELES

90127, velká výzkumná infrastruktura

Název: CIISB II

Přiložené soubory

s42003-022-03793-z.pdf Verze souboru

Citovat

GRYBCHUK, Danyil; Michaela PROCHÁZKOVÁ; Tibor FÜZIK; Aleksandras KONOVALOVAS; Saulius SERVA; Vyacheslav YURCHENKO a Pavel PLEVKA. Structures of L-BC virus and its open particle provide insight into Totivirus capsid assembly. Communications Biology. Nature Research, 2022, roč. 5, č. 1, s. 847-856. ISSN 2399-3642. Dostupné z: https://doi.org/10.1038/s42003-022-03793-z.

@article{2228362,
   author = {Grybchuk, Danyil and Procházková, Michaela and Füzik, Tibor and Konovalovas, Aleksandras and Serva, Saulius and Yurchenko, Vyacheslav and Plevka, Pavel},
   article_number = {1},
   doi = {https://doi.org/10.1038/s42003-022-03793-z},
   keywords = {Animals; Capsid; Capsid Proteins; Cryoelectron Microscopy; Totivirus; Viruses},
   language = {eng},
   issn = {2399-3642},
   journal = {Communications Biology},
   title = {Structures of L-BC virus and its open particle provide insight into Totivirus capsid assembly},
   url = {https://www.nature.com/articles/s42003-022-03793-z},
   volume = {5},
   year = {2022}
}

TY  - JOUR
ID  - 2228362
AU  - Grybchuk, Danyil - Procházková, Michaela - Füzik, Tibor - Konovalovas, Aleksandras - Serva, Saulius - Yurchenko, Vyacheslav - Plevka, Pavel
PY  - 2022
TI  - Structures of L-BC virus and its open particle provide insight into Totivirus capsid assembly
JF  - Communications Biology
VL  - 5
IS  - 1
SP  - 847
EP  - 847
PB  - Nature Research
SN  - 23993642
KW  - Animals
KW  - Capsid
KW  - Capsid Proteins
KW  - Cryoelectron Microscopy
KW  - Totivirus
KW  - Viruses
UR  - https://www.nature.com/articles/s42003-022-03793-z
N2  - L-BC virus persists in the budding yeast Saccharomyces cerevisiae, whereas other viruses from the family Totiviridae infect a diverse group of organisms including protists, fungi, arthropods, and vertebrates. The presence of totiviruses alters the fitness of the host organisms, for example, by maintaining the killer system in yeast or increasing the virulence of Leishmania guyanensis. Despite the importance of totiviruses for their host survival, there is limited information about Totivirus structure and assembly. Here we used cryo-electron microscopy to determine the structure of L-BC virus to a resolution of 2.9 angstrom. The L-BC capsid is organized with icosahedral symmetry, with each asymmetric unit composed of two copies of the capsid protein. Decamers of capsid proteins are stabilized by domain swapping of the C-termini of subunits located around icosahedral fivefold axes. We show that capsids of 9% of particles in a purified L-BC sample were open and lacked one decamer of capsid proteins. The existence of the open particles together with domain swapping within a decamer provides evidence that Totiviridae capsids assemble from the decamers of capsid proteins. Furthermore, the open particles may be assembly intermediates that are prepared for the incorporation of the virus (+) strand RNA. A 2.9 angstrom resolution structure of the L-BC virus provides insight into the contacts between capsid proteins and the mechanism of capsid assembly.
ER  -

GRYBCHUK, Danyil; Michaela PROCHÁZKOVÁ; Tibor FÜZIK; Aleksandras KONOVALOVAS; Saulius SERVA; Vyacheslav YURCHENKO a Pavel PLEVKA. Structures of L-BC virus and its open particle provide insight into Totivirus capsid assembly. \textit{Communications Biology}. Nature Research, 2022, roč.~5, č.~1, s.~847-856. ISSN~2399-3642. Dostupné z: https://doi.org/10.1038/s42003-022-03793-z.

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