Capsid structure of bacteriophage ΦKZ provides insights into assembly and stabilization of jumbo phages

Yashan Yang, Qianqian Shao, Mingcheng Guo, Lin Han, Xinyue Zhao, Aohan Wang, Xiangyun Li, Bo Wang, Ji-An Pan, Zhenguo Chen, Andrei Fokine, Lei Sun () and Qianglin Fang ()
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Yashan Yang: School of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University
Qianqian Shao: School of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University
Mingcheng Guo: School of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University
Lin Han: Fudan University
Xinyue Zhao: School of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University
Aohan Wang: School of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University
Xiangyun Li: School of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University
Bo Wang: Shenzhen Campus of Sun Yat-sen University
Ji-An Pan: Shenzhen Campus of Sun Yat-sen University
Zhenguo Chen: Fudan University
Andrei Fokine: Purdue University
Lei Sun: Fudan University
Qianglin Fang: School of Public Health (Shenzhen), Shenzhen Campus of Sun Yat-sen University

Nature Communications, 2024, vol. 15, issue 1, 1-12

Abstract: Abstract Jumbo phages are a group of tailed bacteriophages with large genomes and capsids. As a prototype of jumbo phage, ΦKZ infects Pseudomonas aeruginosa, a multi-drug-resistant (MDR) opportunistic pathogen leading to acute or chronic infection in immunocompromised individuals. It holds potential to be used as an antimicrobial agent and as a model for uncovering basic phage biology. Although previous low-resolution structural studies have indicated that jumbo phages may have more complicated capsid structures than smaller phages such as HK97, the detailed structures and the assembly mechanism of their capsids remain largely unknown. Here, we report a 3.5-Å-resolution cryo-EM structure of the ΦKZ capsid. The structure unveiled ten minor capsid proteins, with some decorating the outer surface of the capsid and the others forming a complex network attached to the capsid’s inner surface. This network seems to play roles in driving capsid assembly and capsid stabilization. Similar mechanisms of capsid assembly and stabilization are probably employed by many other jumbo viruses.

Date: 2024
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DOI: 10.1038/s41467-024-50811-1

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