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Review

Terminase Large Subunit Provides a New Drug Target for Herpesvirus Treatment

by 1,2,3,†, 1,2,3,*,†, 1,2,3, 1,2,3, 1,2,3, 1,2,3, 1,2,3, 1,2,3, 1,2,3, 1,2,3, 1,2,3, 1,2,3, 1,2,3, 2,3 and 1,2,3,*
1
Institute of Preventive Veterinary Medicine, Sichuan Agricultural University, Chengdu 611130, Sichuan, China
2
Research Center of Avian Diseases, College of Veterinary Medicine, Sichuan Agricultural University, Chengdu 611130, Sichuan, China
3
Key Laboratory of Animal Disease and Human Health of Sichuan Province, Chengdu 611130, Sichuan, China
*
Authors to whom correspondence should be addressed.
These authors contributed equally to this work.
Received: 3 December 2018 / Revised: 23 February 2019 / Accepted: 27 February 2019 / Published: 5 March 2019
(This article belongs to the Special Issue Recent Advances in Herpesviruses Research: What's in the Pipeline?)
Herpesvirus infection is an orderly, regulated process. Among these viruses, the encapsidation of viral DNA is a noteworthy link; the entire process requires a powered motor that binds to viral DNA and carries it into the preformed capsid. Studies have shown that this power motor is a complex composed of a large subunit, a small subunit, and a third subunit, which are collectively known as terminase. The terminase large subunit is highly conserved in herpesvirus. It mainly includes two domains: the C-terminal nuclease domain, which cuts the viral concatemeric DNA into a monomeric genome, and the N-terminal ATPase domain, which hydrolyzes ATP to provide energy for the genome cutting and transfer activities. Because this process is not present in eukaryotic cells, it provides a reliable theoretical basis for the development of safe and effective anti-herpesvirus drugs. This article reviews the genetic characteristics, protein structure, and function of the herpesvirus terminase large subunit, as well as the antiviral drugs that target the terminase large subunit. We hope to provide a theoretical basis for the prevention and treatment of herpesvirus. View Full-Text
Keywords: herpesvirus; terminase large subunit; ATPase; nuclease; DNA packaging; antiviral drug herpesvirus; terminase large subunit; ATPase; nuclease; DNA packaging; antiviral drug
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MDPI and ACS Style

Yang, L.; Yang, Q.; Wang, M.; Jia, R.; Chen, S.; Zhu, D.; Liu, M.; Wu, Y.; Zhao, X.; Zhang, S.; Liu, Y.; Yu, Y.; Zhang, L.; Chen, X.; Cheng, A. Terminase Large Subunit Provides a New Drug Target for Herpesvirus Treatment. Viruses 2019, 11, 219. https://0-doi-org.brum.beds.ac.uk/10.3390/v11030219

AMA Style

Yang L, Yang Q, Wang M, Jia R, Chen S, Zhu D, Liu M, Wu Y, Zhao X, Zhang S, Liu Y, Yu Y, Zhang L, Chen X, Cheng A. Terminase Large Subunit Provides a New Drug Target for Herpesvirus Treatment. Viruses. 2019; 11(3):219. https://0-doi-org.brum.beds.ac.uk/10.3390/v11030219

Chicago/Turabian Style

Yang, Linlin, Qiao Yang, Mingshu Wang, Renyong Jia, Shun Chen, Dekang Zhu, Mafeng Liu, Ying Wu, Xinxin Zhao, Shaqiu Zhang, Yunya Liu, Yanling Yu, Ling Zhang, Xiaoyue Chen, and Anchun Cheng. 2019. "Terminase Large Subunit Provides a New Drug Target for Herpesvirus Treatment" Viruses 11, no. 3: 219. https://0-doi-org.brum.beds.ac.uk/10.3390/v11030219

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