J 2023

Structure of the Borrelia Bacteriophage uBB1 Procapsid

RUMNIEKS, Janis, Tibor FÜZIK a Kaspars TARS

Základní údaje

Originální název

Structure of the Borrelia Bacteriophage uBB1 Procapsid

Autoři

RUMNIEKS, Janis (garant), Tibor FÜZIK (703 Slovensko, domácí) a Kaspars TARS

Vydání

Journal of Molecular Biology, LONDON, ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, 2023, 0022-2836

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Velká Británie a Severní Irsko

Utajení

není předmětem státního či obchodního tajemství

Odkazy

Impakt faktor

Impact factor: 5.600 v roce 2022

Kód RIV

RIV/00216224:14740/23:00133565

Organizační jednotka

Středoevropský technologický institut

UT WoS

001116481000001

Klíčová slova anglicky

cryo-EM; virus assembly; portal; scaffold; capsid

Štítky

Příznaky

Mezinárodní význam, Recenzováno
Změněno: 18. 10. 2024 14:19, Ing. Jana Kuchtová

Anotace

V originále

Bacteriophages of Borrelia burgdorferi are a biologically important but under-investigated feature of the Lyme disease-causing spirochete. No virulent borrelial viruses have been identified, but all B. burgdorferi isolates carry a prophage 9BB1 as resident circular plasmids. Like its host, the 9BB1 phage is quite distinctive and shares little sequence similarity with other known bacteriophages. We expressed 9BB1 head morphogenesis proteins in Escherichia coli which resulted in assembly of homogeneous prolate procapsid structures and used cryo-electron microscopy to determine the three-dimensional structure of these particles. The 9BB1 procapsids consist of 415 copies of the major capsid protein and an equal combined number of three homologous capsid decoration proteins that form trimeric knobs on the outside of the particle. One of the end vertices of the particle is occupied by a portal assembled from twelve copies of the portal protein. The 9BB1 scaffolding protein is entirely a-helical and has an elongated shape with a small globular domain in the middle. Within the tubular section of the procapsid, the internal scaffold is built of stacked rings, each composed of 32 scaffolding protein molecules, which run in opposite directions from both caps with a heterogeneous part in the middle. Inside the portal-containing cap, the scaffold is organized asymmetrically with ten scaffolding protein molecules bound to the portal. The 9BB1 procapsid structure provides better insight into the vast structural diversity of bacteriophages and presents clues of how elongated bacteriophage particles might be assembled.(c) 2023 The Authors. Published by Elsevier Ltd.

Návaznosti

871037, interní kód MU
Název: iNEXT-Discovery: Infrastructure for transnational access and discovery in integrated structural biology (Akronym: iNEXT- Discovery)
Investor: Evropská unie, iNEXT-Discovery: Infrastructure for transnational access and discovery in integrated structural biology, RI Research Infrastructures (Excellent Science)
90242, velká výzkumná infrastruktura
Název: CIISB III