7WN7

Crystal structure of HearNPV P26

Summary for 7WN7

• Entry DOI: 10.2210/pdb7wn7/pdb
• Descriptor: p26, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: nuclease, hydrolase
• Biological source: Helicoverpa armigera nucleopolyhedrovirus G4
• Total number of polymer chains: 2
• Total formula weight: 68423.54

Authors

Kuang, W.,Hu, Z.,Gong, P. (deposition date: 2022-01-17, release date: 2022-11-23, Last modification date: 2024-05-29)

Primary citation

Yin, M.,Kuang, W.,Wang, Q.,Wang, X.,Yuan, C.,Lin, Z.,Zhang, H.,Deng, F.,Jiang, H.,Gong, P.,Zou, Z.,Hu, Z.,Wang, M.
Dual roles and evolutionary implications of P26/poxin in antagonizing intracellular cGAS-STING and extracellular melanization immunity.
Nat Commun, 13:6934-6934, 2022

PubMed Abstract: P26, a homolog of the viral-encoded nuclease poxin that neutralizes the cGAS-STING innate immunity, is widely distributed in various invertebrate viruses, lepidopteran insects, and parasitoid wasps. P26/poxin from certain insect viruses also retains protease activity, though its biological role remains unknown. Given that many P26s contain a signal peptide, it is surmised that P26 may possess certain extracellular functions. Here, we report that a secretory baculoviral P26 suppresses melanization, a prominent insect innate immunity against pathogen invasion. P26 targets the cofactor of a prophenoloxidase-activating protease, and its inhibitory function is independent of nuclease activity. The analysis of P26/poxin homologs from different origins suggests that the ability to inhibit the extracellular melanization pathway is limited to P26s with a signal peptide and not shared by the homologs without it. These findings highlight the independent evolution of a single viral suppressor to perform dual roles in modulating immunity during virus-host adaptation.

PubMed: 36376305
DOI: 10.1038/s41467-022-34761-0

Experimental method

X-RAY DIFFRACTION (1.9 Å)