Zika virus (ZIKV) is an important human pathogen associated with severe neurological disorders. Ubiquitination of viral proteins has diverse roles in viral life cycle and pathogenesis. Here, we found that perturbation of ubiquitin-proteasome system significantly suppressed production of infectious viral particles. Moreover, we demonstrated that ZIKV precursor membrane (prM) protein underwent ubiquitination and proteasomal degradation. Furthermore, we showed that co-expression of E protein with ubiquitination-deficient prM-6 K/6R mutant protein did not affect translocation of viral proteins into endoplasmic reticulum and trans-Golgi networks. Intriguingly, the co-expression of E and prM-6 K/6R mutant proteins led to formation of relatively aggregated viral protein complexes and resulted in diminishing secretion of viral proteins as compared to wild-type prM. Collectively, these results suggest that ubiquitinated ZIKV prM protein contributes to the release of viral proteins and provide a new insight into the mechanism involved in ZIKV replication biology.

寨卡病毒（ZIKV）是与严重的神经系统疾病有关的重要人类病原体。病毒蛋白的泛素化在病毒的生命周期和发病机理中具有多种作用。在这里，我们发现泛素-蛋白酶体系统的干扰显着抑制了感染性病毒颗粒的产生。此外，我们证明ZIKV前体膜（prM）蛋白经历了泛素化和蛋白酶体降解。此外，我们表明E蛋白与泛素化缺陷prM-6 K / 6R突变蛋白的共表达不会影响病毒蛋白向内质网和高尔基体网络的转运。有趣的是 与野生型prM相比，E和prM-6 K / 6R突变蛋白的共表达导致形成相对聚集的病毒蛋白复合物，并导致病毒蛋白的分泌减少。总的来说，这些结果表明泛素化的ZIKV prM蛋白有助于病毒蛋白的释放，并为ZIKV复制生物学涉及的机制提供了新的见识。