Litcius/Paper detail

The crustacean DNA virus tegument protein VP26 binds to SNAP29 to inhibit SNARE complex assembly and autophagic degradation

Ling-ke Liu, Jiu-Ting Jian, Shan‐Shan Jing, Ruilin Gao, Xiao-Dong Chi, Geng Tian, Hai‐Peng Liu

2024Journal of Virology18 citationsDOIOpen Access PDF

Abstract

White spot syndrome virus (WSSV) is one of the largest animal DNA viruses in terms of its genome size and has caused huge economic losses in the farming of crustaceans such as shrimp and crayfish. Detailed knowledge of WSSV-host interactions is still lacking, particularly regarding viral escape from host immune clearance. Intriguingly, we found that the presence of WSSV-VP26 might inhibit the autophagic degradation of WSSV in vivo in the crustacean species red claw crayfish. Importantly, this study is the first to show that viral protein VP26 functions as a core factor to benefit WSSV escape by disrupting the assembly of the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex, which is necessary for the proposed fusion of autophagosomes with lysosomes for subsequent degradation. These findings highlight a novel mechanism of DNA virus evasion by blocking SNARE complex assembly and identify viral VP26 as a key candidate for anti-WSSV targeting.

Topics & Concepts

BiologyCell biologyAutophagosomeAutophagyVirusWhite spot syndromeDNA virusViral replicationLysosomeViral tegumentVirologyGeneGeneticsBiochemistryApoptosisEnzymeGenomeMosquito-borne diseases and controlAutophagy in Disease and TherapyInsect symbiosis and bacterial influences
The crustacean DNA virus tegument protein VP26 binds to SNAP29 to inhibit SNARE complex assembly and autophagic degradation | Litcius