Structure of the Borrelia Bacteriophage uBB1 Procapsid

J 2023

Structure of the Borrelia Bacteriophage uBB1 Procapsid

RUMNIEKS, Janis, Tibor FÜZIK and Kaspars TARS

Basic information

Original name

Structure of the Borrelia Bacteriophage uBB1 Procapsid

Authors

RUMNIEKS, Janis (guarantor), Tibor FÜZIK (703 Slovakia, belonging to the institution) and Kaspars TARS

Edition

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

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10608 Biochemistry and molecular biology

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 5.600 in 2022

RIV identification code

RIV/00216224:14740/23:00133565

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1016/j.jmb.2023.168323

UT WoS

001116481000001

Keywords in English

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

Abstract

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.

Links

871037, interní kód MU

Name: iNEXT-Discovery: Infrastructure for transnational access and discovery in integrated structural biology (Acronym: iNEXT- Discovery)

Investor: European Union, RI Research Infrastructures (Excellent Science)

90242, large research infrastructures

Name: CIISB III

Citovat

RUMNIEKS, Janis, Tibor FÜZIK and Kaspars TARS. Structure of the Borrelia Bacteriophage uBB1 Procapsid. Journal of Molecular Biology. LONDON: ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, 2023, vol. 435, No 24, p. 1-18. ISSN 0022-2836. Available from: https://dx.doi.org/10.1016/j.jmb.2023.168323.

@article{2375358,
   author = {Rumnieks, Janis and Füzik, Tibor and Tars, Kaspars},
   article_location = {LONDON},
   article_number = {24},
   doi = {http://dx.doi.org/10.1016/j.jmb.2023.168323},
   keywords = {cryo-EM; virus assembly; portal; scaffold; capsid},
   language = {eng},
   issn = {0022-2836},
   journal = {Journal of Molecular Biology},
   title = {Structure of the Borrelia Bacteriophage uBB1 Procapsid},
   url = {https://www.sciencedirect.com/science/article/pii/S0022283623004345?via%3Dihub},
   volume = {435},
   year = {2023}
}

TY  - JOUR
ID  - 2375358
AU  - Rumnieks, Janis - Füzik, Tibor - Tars, Kaspars
PY  - 2023
TI  - Structure of the Borrelia Bacteriophage uBB1 Procapsid
JF  - Journal of Molecular Biology
VL  - 435
IS  - 24
SP  - 1-18
EP  - 1-18
PB  - ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
SN  - 00222836
KW  - cryo-EM
KW  - virus assembly
KW  - portal
KW  - scaffold
KW  - capsid
UR  - https://www.sciencedirect.com/science/article/pii/S0022283623004345?via%3Dihub
N2  - 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.
ER  -

RUMNIEKS, Janis, Tibor FÜZIK and Kaspars TARS. Structure of the Borrelia Bacteriophage uBB1 Procapsid. \textit{Journal of Molecular Biology}. LONDON: ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD, 2023, vol.~435, No~24, p.~1-18. ISSN~0022-2836. Available from: https://dx.doi.org/10.1016/j.jmb.2023.168323.

Detailed Information on Publication Record