期刊
VETERINARY MICROBIOLOGY
卷 272, 期 -, 页码 -出版社
ELSEVIER
DOI: 10.1016/j.vetmic.2022.109517
关键词
Pseudorabies virus; DNA polymerase; Catalytic subunit UL30; Accessory subunit UL42; Subunit interaction
资金
- National Natural Science Foundation of China [31873012]
This study identified the key domains that mediate the interaction between PRV UL30 and UL42, providing potential targets for designing a novel intervention strategy against PRV infection. The findings also support the concept that herpesvirus DNA polymerase subunits utilize their extreme carboxy-terminal domains to interact with their accessory subunits, suggesting the opportunity of designing novel antiviral agents against herpesvirus infection through disruption of the polymerase subunit interactions.
Pseudorabies virus (PRV) is a ubiquitous and economically important swine alphaherpesvirus that causes devastating swine diseases worldwide. PRV-encoded DNA-dependent DNA polymerase, comprised of the cata-lytic subunit UL30 and the accessory subunit UL42, is essential for viral replication. PRV UL30 and UL42 act as a heterodimer with UL30 harboring inherent DNA polymerase activity and UL42 conferring processivity on the DNA polymerase holoenzyme. The formation of PRV UL30/UL42 heterodimer holoenzyme through protein -protein interactions is indispensable for viral replication. In work described here, we defined the key domains that mediate PRV UL30/UL42 interaction, and found that the 41 carboxy-terminal amino acids region of PRV UL30 is critical for its interaction with UL42. Intriguingly, a synthetic peptide corresponding to these 41 carboxy-terminal amino acid residues efficiently disrupted PRV UL30/UL42 interaction through competitively binding to UL42. These findings suggest that the peptides from the PRV DNA polymerase UL30/UL42 subunit interface may represent potential targets for designing a novel intervention strategy against PRV infection. This work further strengthens the concept that the herpesvirus DNA polymerase catalytic subunits utilize their extreme carboxy-terminal domains as a conserved mechanism to associate with their cognate accessory subunits, providing us the opportunity of designing novel antiviral agents against herpesvirus infection through disruption of the herpesvirus DNA polymerase subunit interactions.
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