Human ANP32A/B are SUMOylated and utilized by avian influenza virus NS2 protein to overcome species-specific restriction
Human ANP32A/B (huANP32A/B) poorly support the polymerase activity of avian influenza viruses (AIVs), thereby limiting interspecies transmission of AIVs from birds to humans. The SUMO-interacting motif (SIM) within NS2 promotes the adaptation of AIV polymerase to huANP32A/B via a yet undisclosed mechanism. Here we show that huANP32A/B are SUMOylated by the E3 SUMO ligase PIAS2α, and deSUMOylated by SENP1. SUMO modification of huANP32A/B results in the recruitment of NS2, thereby facilitating huANP32A/B-supported AIV polymerase activity. Such a SUMO-dependent recruitment of NS2 is mediated by its association with huANP32A/B via the SIM-SUMO interaction module, where K68/K153-SUMO in huANP32A or K68/K116-SUMO in huANP32B interacts with the NS2-SIM. The SIM-SUMO-mediated interactions between NS2 and huANP32A/B function to promote AIV polymerase activity by positively regulating AIV vRNP-huANP32A/B interactions and AIV vRNP assembly. Our study offers insights into the mechanism of NS2-SIM in facilitating AIVs adaptation to mammals.
Authors
- Mengmeng Yu (ORCID: https://orcid.org/0000-0001-8656-0188)
- Liuke Sun (ORCID: https://orcid.org/0000-0002-5118-4992)
- Xiaojun Wang (ORCID: https://orcid.org/0000-0003-4521-4099)
- Xuefeng Wang (ORCID: https://orcid.org/0000-0002-5564-2487)
- Huiling Ren (ORCID: https://orcid.org/0000-0002-6043-1414)
- Xing Guo (ORCID: https://orcid.org/0000-0001-9496-2267)
Institutions
- Chinese Academy of Agricultural Sciences (CN)
- Harbin Veterinary Research Institute (CN)
Publication Details
- Journal
- Nature Communications
- Published
- 2024-12-30
- DOI
- https://doi.org/10.1038/s41467-024-55034-y
- Citations
- 6
- Primary Topic
- Influenza Virus Research Studies
- Type
- article
- Field-Weighted Citation Impact
- 2.32
Funders
- National Natural Science Foundation of China
- Natural Science Foundation of Heilongjiang Province
- Chinese Academy of Agricultural Sciences