Abstract
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.
Highlights
The members of Herpesviridae are double-stranded DNA viruses
During the viral DNA packaging process, the three terminase subunits form a complex in the cytoplasm and enter the nucleus to perform the functions [34,35]. pUL15 and its homologs are generally considered to be terminase large subunits that function as nuclease to cleave the viral concatemeric DNA [22]
Previous studies have shown that herpes simplex virus 1 (HSV-1) pUL15 is a catalytic element of the terminase complex and mainly consists of two domains: the N-terminal ATPase domain and the C-terminal nuclease domain [50] (Figure 4A)
Summary
The members of Herpesviridae are double-stranded DNA (dsDNA) viruses. According to the International Committee on Taxonomy of Viruses (ICTV), in April 2018 [1], the family Herpesviridae was divided into three subfamilies (Alphaherpesvirinae, Betaherpesvirinae, and Gammaherpesvirinae) and an unassigned genus thought to have diverged from a common ancestor 400 million years ago [2,3]. PUL15, pUL28, and pUL33 are believed to have terminase complex functions that cleave the head-to-tail linked viral concatemeric DNA at a precise location to release unit-length genomes and package the DNA into preformed capsids [20,21,22,23]. This mechanism exists in prokaryotic and eukaryotic dsDNA viruses, such as bacteriophages and herpesviruses [24,25,26,27,28]
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