Structural highlights
FunctionG7P_BPF1 May initiate with G9P the virion concomitant assembly-budding process, by interacting with the packaging signal of the viral genome. The assembly-budding takes place at the host inner membrane. In turn, G7P and G9P are present at the end of the filamentous virion that emerges first from the bacterial host (By similarity). Publication Abstract from PubMedPhages are viruses that infect bacteria and dominate every ecosystem on our planet. As well as impacting microbial ecology, physiology and evolution, phages are exploited as tools in molecular biology and biotechnology. This is particularly true for the Ff (f1, fd or M13) phages, which represent a widely distributed group of filamentous viruses. Over nearly five decades, Ffs have seen an extraordinary range of applications, yet the complete structure of the phage capsid and consequently the mechanisms of infection and assembly remain largely mysterious. In this work, we use cryo-electron microscopy and a highly efficient system for production of short Ff-derived nanorods to determine a structure of a filamentous virus including the tips. We show that structure combined with mutagenesis can identify phage domains that are important in bacterial attack and for release of new progeny, allowing new models to be proposed for the phage lifecycle. Cryo-electron microscopy of the f1 filamentous phage reveals insights into viral infection and assembly.,Conners R, Leon-Quezada RI, McLaren M, Bennett NJ, Daum B, Rakonjac J, Gold VAM Nat Commun. 2023 May 11;14(1):2724. doi: 10.1038/s41467-023-37915-w. PMID:37169795[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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