James L. Van Etten , Irina V. Agarkova , David D. Dunigan , Qianqian Shao , Qianglin Fang
{"title":"氯病毒PBCV-1的新结构","authors":"James L. Van Etten , Irina V. Agarkova , David D. Dunigan , Qianqian Shao , Qianglin Fang","doi":"10.1016/j.virol.2025.110552","DOIUrl":null,"url":null,"abstract":"<div><div>The large plaque-forming chloroviruses infect isolates of eukaryotic chlorella-like green algae. Initial cryo-electron microscopy (cryo-EM) studies revealed that PBCV-1 was icosahedral, with a multilaminate shell surrounding an electron-dense core, and that PBCV-1 particles measured about 1900 Å in diameter with a triangulation number of 169d. However, as described in this review cryo-EM procedures have improved and PBCV-1 is more complex than originally described. A five-fold symmetry reconstruction of cryo-EM images at 8.5 Å revealed that the virus contains a unique vertex with a spike-structure and an internal single lipid bi-layered membrane. Improvement to 3.5 Å resolution revealed that the capsid contains 30 virus-encoded proteins and that it contains six different types of capsomers. The outer surface of three of the six types of capsomers are attached to fiber structures.</div></div>","PeriodicalId":23666,"journal":{"name":"Virology","volume":"608 ","pages":"Article 110552"},"PeriodicalIF":2.8000,"publicationDate":"2025-04-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Emerging structure of chlorovirus PBCV-1\",\"authors\":\"James L. Van Etten , Irina V. Agarkova , David D. Dunigan , Qianqian Shao , Qianglin Fang\",\"doi\":\"10.1016/j.virol.2025.110552\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><div>The large plaque-forming chloroviruses infect isolates of eukaryotic chlorella-like green algae. Initial cryo-electron microscopy (cryo-EM) studies revealed that PBCV-1 was icosahedral, with a multilaminate shell surrounding an electron-dense core, and that PBCV-1 particles measured about 1900 Å in diameter with a triangulation number of 169d. However, as described in this review cryo-EM procedures have improved and PBCV-1 is more complex than originally described. A five-fold symmetry reconstruction of cryo-EM images at 8.5 Å revealed that the virus contains a unique vertex with a spike-structure and an internal single lipid bi-layered membrane. Improvement to 3.5 Å resolution revealed that the capsid contains 30 virus-encoded proteins and that it contains six different types of capsomers. The outer surface of three of the six types of capsomers are attached to fiber structures.</div></div>\",\"PeriodicalId\":23666,\"journal\":{\"name\":\"Virology\",\"volume\":\"608 \",\"pages\":\"Article 110552\"},\"PeriodicalIF\":2.8000,\"publicationDate\":\"2025-04-22\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Virology\",\"FirstCategoryId\":\"3\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0042682225001655\",\"RegionNum\":3,\"RegionCategory\":\"医学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q3\",\"JCRName\":\"VIROLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Virology","FirstCategoryId":"3","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0042682225001655","RegionNum":3,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"VIROLOGY","Score":null,"Total":0}
The large plaque-forming chloroviruses infect isolates of eukaryotic chlorella-like green algae. Initial cryo-electron microscopy (cryo-EM) studies revealed that PBCV-1 was icosahedral, with a multilaminate shell surrounding an electron-dense core, and that PBCV-1 particles measured about 1900 Å in diameter with a triangulation number of 169d. However, as described in this review cryo-EM procedures have improved and PBCV-1 is more complex than originally described. A five-fold symmetry reconstruction of cryo-EM images at 8.5 Å revealed that the virus contains a unique vertex with a spike-structure and an internal single lipid bi-layered membrane. Improvement to 3.5 Å resolution revealed that the capsid contains 30 virus-encoded proteins and that it contains six different types of capsomers. The outer surface of three of the six types of capsomers are attached to fiber structures.
期刊介绍:
Launched in 1955, Virology is a broad and inclusive journal that welcomes submissions on all aspects of virology including plant, animal, microbial and human viruses. The journal publishes basic research as well as pre-clinical and clinical studies of vaccines, anti-viral drugs and their development, anti-viral therapies, and computational studies of virus infections. Any submission that is of broad interest to the community of virologists/vaccinologists and reporting scientifically accurate and valuable research will be considered for publication, including negative findings and multidisciplinary work.Virology is open to reviews, research manuscripts, short communication, registered reports as well as follow-up manuscripts.