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CryoEM structure of the central filamentous region of the f1 filamentous bacteriophage, consisting of the major capsid protein pVIIICryoEM structure of the central filamentous region of the f1 filamentous bacteriophage, consisting of the major capsid protein pVIII
Structural highlights
FunctionCAPSD_BPF1 Self assembles to form a helical capsid wrapping up the viral genomic DNA. The capsid displays a filamentous structure with a length of 760-1950 nm and a width of 6-8 nm. The virion assembly and budding take place at the host inner membrane (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. See AlsoReferences
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