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作 者:Yun-Xiao Zheng Lei Wang Wei-Sha Kong Hong Chen Xue-Ning Wang Qingfeng Meng Hai-Nan Zhang Shu-Juan Guo He-Wei Jiang Sheng-Ce Tao
出 处:《Acta Biochimica et Biophysica Sinica》2021年第9期1134-1141,共8页生物化学与生物物理学报(英文版)
基 金:the grants from the National Key Research and Development Program of China(No.2016YFA0500600);the National Natural Science Foundation of China(Nos.31900112,21907065,31970130,and 31670831).
摘 要:Severe acute respiratory syndrome coronavirus 2(SARS-CoV-2)has become a global health threat since December 2019,and there is still no highly effective drug to control the pandemic.To facilitate drug target identification for drug development,studies on molecular mechanisms,such as SARS-CoV-2 protein interactions,are urgently needed.In this study,we focused on Nsp2,a non-structural protein with largely unknown function and mechanism.The interactome of Nsp2 was revealed through the combination of affinity purification mass spectrometry(AP-MS)and stable isotope labeling by amino acids in cell culture(SILAC),and 84 proteins of high-confidence were identified.Gene ontology analysis demonstrated that Nsp2-interacting proteins are involved in several biological processes such as endosome transport and translation.Network analysis generated two clusters,including ribosome assembly and vesicular transport.Bio-layer interferometry(BLI)assay confirmed the bindings between Nsp2-and 4-interacting proteins,i.e.STAU2(Staufen2),HNRNPLL,ATP6V1B2,and RAP1GDS1(SmgGDS),which were randomly selected from the list of 84 proteins.Our findings provide insights into the Nsp2–host interplay and indicate that Nsp2 may play important roles in SARS-CoV-2 infection and serve as a potential drug target for anti-SARS-CoV-2 drug development.
关 键 词:NSP2 SARS-CoV-2 protein-protein interaction AP-MS SILAC
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