iProXProteomicsZeyu SunSevere Acute Respiratory Syndrome Coronavirus 2http://www.iprox.org/page/project.html?id=IPX0002757000zeyusun@zju.edu.cnZhejiang UniversityiProXThe coronavirus disease 2019 (COVID-19) pandemic has led to worldwide efforts to understand the biological traits of the newly identified human coronavirus (HCoV-19) virus. In this mass spectrometry (MS)-based study, we reveal that out of 21 possible glycosites in the HCoV-19 spike protein (S protein), 20 are completely occupied by <i>N</i>-glycans, predominantly of the oligomannose type. All seven glycosylation sites in human angiotensin I converting enzyme 2 (hACE2) were found to be completely occupied, mainly by complex <i>N</i>-glycans. However, glycosylation did not directly contribute to the binding affinity between HCoV-19 S protein and hACE2. Additional post-translational modification (PTM) was identified, including multiple methylated sites in both proteins and multiple sites with hydroxylproline in hACE2. Refined structural models of HCoV-19 S protein and hACE2 were built by adding <i>N</i>-glycan and PTMs to recently published cryogenic electron microscopy structures. The PTM and glycan maps of HCoV-19 S protein and hACE2 provide additional structural details for studying the mechanisms underlying host attachment and the immune response of HCoV-19, as well as knowledge for developing desperately needed remedies and vaccines.Mass Spectrometry Analysis of Newly Emerging Coronavirus HCoV-19 Spike Protein and Human ACE2 Reveals Camouflaging Glycans and Unique Post-Translational Modifications.Sun Zeyu Z, Ren Keyi K, Zhang Xing X, Chen Jinghua J, Jiang Zhengyi Z, Jiang Jing J, Ji Feiyang F, Ouyang Xiaoxi X, Li Lanjuan LfalseMS characterization of SARS-CoV-2 NCP PTM profileGlycosylation and PTM profile of NCP from SARS-CoV-2Wed Apr 14 00:00:00 BST 2021PXD025404269704932904601