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-Structure paper
タイトル | Cryo-electron microscopy of the f1 filamentous phage reveals insights into viral infection and assembly. |
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ジャーナル・号・ページ | Nat Commun, Vol. 14, Issue 1, Page 2724, Year 2023 |
掲載日 | 2023年5月11日 |
著者 | Rebecca Conners / Rayén Ignacia León-Quezada / Mathew McLaren / Nicholas J Bennett / Bertram Daum / Jasna Rakonjac / Vicki A M Gold / |
PubMed 要旨 | Phages 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 ...Phages 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. |
リンク | Nat Commun / PubMed:37169795 / PubMed Central |
手法 | EM (単粒子) / EM (らせん対称) |
解像度 | 2.58 - 2.97 Å |
構造データ | EMDB-15831, PDB-8b3o: EMDB-15832, PDB-8b3p: EMDB-15833, PDB-8b3q: |
由来 |
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キーワード | VIRUS (ウイルス) / Viral proteins (ウイルスタンパク質) / Infection (感染) / assembly / capsid (カプシド) |