Ubiquitination is a critical posttranslational modification that regulates host immune responses to pathogens. In this study, we investigated the ubiquitination of hemocyanin (PvHMC [Penaeus vannamei hemocyanin]) mediated by the mitochondrial E3 ubiquitin ligase (PvMulan) in shrimp Penaeus vannamei. We characterized distinct ubiquitination patterns of PvHMC in response to different pathogen challenges, both in vitro and in vivo. Specifically, we found that Vibrio parahaemolyticus infection led to an increase in PvMulan, which resulted in K48-linked ubiquitination and subsequent proteasomal degradation of PvHMC. In contrast, PvMulan primarily enhanced the SUMOylation of PvHMC, bolstering its immune functions against white spot syndrome virus challenges. Inhibition of PvMulan-mediated PvHMC ubiquitination significantly affected the proliferation of V. parahaemolyticus and the survival rate of infected shrimps. This study sheds light on the role of hemocyanin ubiquitination in immune regulation, illustrating its dual function in response to distinct pathogens.



Summary

This study investigates how the E3 ubiquitin ligase PvMulan in shrimp Penaeus vannamei regulates hemocyanin (PvHMC) ubiquitination in response to pathogens. Vibrio parahaemolyticus infection increases PvMulan, leading to K48-linked ubiquitination and degradation of PvHMC. Conversely, white spot syndrome virus challenges cause PvMulan to enhance PvHMC SUMOylation, strengthening its immune function. Blocking PvMulan-mediated ubiquitination impacted V. parahaemolyticus proliferation and shrimp survival. These findings demonstrate that PvHMC ubiquitination, mediated by PvMulan, plays a crucial role in the shrimp’s immune response, acting differently against various pathogens.

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