Structures of Qβ virions, virus-like particles, and the Qβ-MurA complex reveal internal coat proteins and the mechanism of host lysis

Proceedings of the National Academy of Sciences of the United States of America
Zhicheng CuiJunjie Zhang

Abstract

In single-stranded RNA bacteriophages (ssRNA phages) a single copy of the maturation protein binds the genomic RNA (gRNA) and is required for attachment of the phage to the host pilus. For the canonical Allolevivirus Qβ the maturation protein, A2, has an additional role as the lysis protein, by its ability to bind and inhibit MurA, which is involved in peptidoglycan biosynthesis. Here, we determined structures of Qβ virions, virus-like particles, and the Qβ-MurA complex using single-particle cryoelectron microscopy, at 4.7-Å, 3.3-Å, and 6.1-Å resolutions, respectively. We identified the outer surface of the β-region in A2 as the MurA-binding interface. Moreover, the pattern of MurA mutations that block Qβ lysis and the conformational changes of MurA that facilitate A2 binding were found to be due to the intimate fit between A2 and the region encompassing the closed catalytic cleft of substrate-liganded MurA. Additionally, by comparing the Qβ virion with Qβ virus-like particles that lack a maturation protein, we observed a structural rearrangement in the capsid coat proteins that is required to package the viral gRNA in its dominant conformation. Unexpectedly, we found a coat protein dimer sequestered in the interior of the viri...Continue Reading

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Citations

Nov 14, 2018·The Journal of Biological Chemistry·Karthik Chamakura, Ry Young
Apr 6, 2019·Annual Review of Biophysics·Reidun Twarock, Peter G Stockley
Jul 3, 2020·PLoS Pathogens·Chihong SongKazuyoshi Murata
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Oct 20, 2020·Current Opinion in Microbiology·Karthik R Chamakura, Ry Young
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