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-Structure paper
タイトル | High-resolution reconstruction of a Jumbo-bacteriophage infecting capsulated bacteria using hyperbranched tail fibers. |
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ジャーナル・号・ページ | Nat Commun, Vol. 13, Issue 1, Page 7241, Year 2022 |
掲載日 | 2022年11月24日 |
著者 | Ruochen Ouyang / Ana Rita Costa / C Keith Cassidy / Aleksandra Otwinowska / Vera C J Williams / Agnieszka Latka / Phill J Stansfeld / Zuzanna Drulis-Kawa / Yves Briers / Daniël M Pelt / Stan J J Brouns / Ariane Briegel / |
PubMed 要旨 | The Klebsiella jumbo myophage ϕKp24 displays an unusually complex arrangement of tail fibers interacting with a host cell. In this study, we combine cryo-electron microscopy methods, protein ...The Klebsiella jumbo myophage ϕKp24 displays an unusually complex arrangement of tail fibers interacting with a host cell. In this study, we combine cryo-electron microscopy methods, protein structure prediction methods, molecular simulations, microbiological and machine learning approaches to explore the capsid, tail, and tail fibers of ϕKp24. We determine the structure of the capsid and tail at 4.1 Å and 3.0 Å resolution. We observe the tail fibers are branched and rearranged dramatically upon cell surface attachment. This complex configuration involves fourteen putative tail fibers with depolymerase activity that provide ϕKp24 with the ability to infect a broad panel of capsular polysaccharide (CPS) types of Klebsiella pneumoniae. Our study provides structural and functional insight into how ϕKp24 adapts to the variable surfaces of capsulated bacterial pathogens, which is useful for the development of phage therapy approaches against pan-drug resistant K. pneumoniae strains. |
リンク | Nat Commun / PubMed:36433970 / PubMed Central |
手法 | EM (単粒子) / EM (らせん対称) |
解像度 | 3.0 - 4.3 Å |
構造データ | EMDB-13862: Jumbo Phage phi-Kp24 empty capsid EMDB-14356: Jumbo Phage phi-Kp24 full capsid EMDB-14357: Jumbo Phage phi-Kp24 extended tail |
由来 |
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キーワード | STRUCTURAL PROTEIN / Jumbo Phage / Klebsiella pneumoniae / tail / sheath / VIRUS / Klebsiella pheumoniae / Capsid |