Key result
SUMO1 modification of the VP1 protein maintained its stability by inhibiting K48-linked ubiquitination and was essential for maintaining IBDV replication.
Why the study?
There is limited understanding regarding the SUMOylation of infectious bursal disease virus viral proteins during infection.
SUMOylation of IBDV VP1 plays an important role in maintaining viral replication by stabilizing the polymerase.
Requires validation beyond avian models before therapeutic consideration; leaves open SUMOylation as a target for polymerase inhibition.
SUMOylation is an extensively discussed posttranslational modification in diverse cellular biological pathways. However, there is limited understanding about SUMOylation of viral proteins of IBDV during infection. In the present study, we revealed a SUMO1 modification of VP1 protein, the RNA-dependent RNA polymerase of avibirnavirus infectious bursal disease virus (IBDV). The required site of VP1 SUMOylation comprised residues 404 I and 406 I of SUMO interaction motif 3, which was essential for maintaining its stability by inhibiting K48-linked ubiquitination. We also showed that IBDV with SUMOylation-deficient VP1 had decreased replication ability. These data demonstrated that the SUMOylation of IBDV VP1 played an important role in maintaining IBDV replication.
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Wu et al. (2019) studied Avibirnavirus infectious bursal disease virus (IBDV) infection. SUMO1 modification of VP1 protein vs. SUMOylation-deficient VP1 was evaluated on VP1 stability and IBDV replication ability. SUMO1 modification of the VP1 protein maintained its stability by inhibiting K48-linked ubiquitination and was essential for maintaining IBDV replication.
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