Structure of the Borrelia Bacteriophage uBB1 Procapsid
| Authors | |
|---|---|
| Year of publication | 2023 |
| Type | Article in Periodical |
| Magazine / Source | Journal of Molecular Biology |
| MU Faculty or unit | |
| Citation | |
| web | https://www.sciencedirect.com/science/article/pii/S0022283623004345?via%3Dihub |
| Doi | http://dx.doi.org/10.1016/j.jmb.2023.168323 |
| Keywords | cryo-EM; virus assembly; portal; scaffold; capsid |
| Description | 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. |
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