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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\n            <jats:sup>404<\/jats:sup>\n            I and\n            <jats:sup>406<\/jats:sup>\n            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.\n          <\/jats:p>","DOI":"10.1128\/jvi.02227-18","type":"journal-article","created":{"date-parts":[[2019,3,6]],"date-time":"2019-03-06T10:26:51Z","timestamp":1551868011000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":22,"title":["SUMO1 Modification Facilitates Avibirnavirus Replication by Stabilizing Polymerase VP1"],"prefix":"10.1128","volume":"93","author":[{"given":"Huansheng","family":"Wu","sequence":"first","affiliation":[{"name":"MOA Key Laboratory of Animal Virology, Department of Veterinary Medicine, Zhejiang University, Hangzhou, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hui","family":"Yang","sequence":"additional","affiliation":[{"name":"MOA Key Laboratory of Animal Virology, Department of Veterinary Medicine, Zhejiang University, Hangzhou, 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