7FJ3

Cryo-EM structure of PRV A-capid

This is a non-PDB format compatible entry.

Summary for 7FJ3

• Entry DOI: 10.2210/pdb7fj3/pdb
• EMDB information: 31612
• Descriptor: Major capsid protein, Triplex capsid protein 2, Triplex capsid protein 1, ... (4 entities in total)
• Functional Keywords: pseudorabies virus, c-capsid, cryo-em, virus
• Biological source: Suid alphaherpesvirus 1; More
• Total number of polymer chains: 51
• Total formula weight: 3227993.48

Authors

Zheng, Q.,Li, S.,Zha, Z.,Sun, H. (deposition date: 2021-08-02, release date: 2022-06-22, Last modification date: 2024-10-23)

Primary citation

Wang, G.,Zha, Z.,Huang, P.,Sun, H.,Huang, Y.,He, M.,Chen, T.,Lin, L.,Chen, Z.,Kong, Z.,Que, Y.,Li, T.,Gu, Y.,Yu, H.,Zhang, J.,Zheng, Q.,Chen, Y.,Li, S.,Xia, N.
Structures of pseudorabies virus capsids.
Nat Commun, 13:1533-1533, 2022

PubMed Abstract: Pseudorabies virus (PRV) is a major etiological agent of swine infectious diseases and is responsible for significant economic losses in the swine industry. Recent data points to human viral encephalitis caused by PRV infection, suggesting that PRV may be able to overcome the species barrier to infect humans. To date, there is no available therapeutic for PRV infection. Here, we report the near-atomic structures of the PRV A-capsid and C-capsid, and illustrate the interaction that occurs between these subunits. We show that the C-capsid portal complex is decorated with capsid-associated tegument complexes. The PRV capsid structure is highly reminiscent of other α-herpesviruses, with some additional structural features of β- and γ-herpesviruses. These results illustrate the structure of the PRV capsid and elucidate the underlying assembly mechanism at the molecular level. This knowledge may be useful for the development of oncolytic agents or specific therapeutics against this arm of the herpesvirus family.

PubMed: 35318331
DOI: 10.1038/s41467-022-29250-3

Experimental method

ELECTRON MICROSCOPY (4.53 Å)