Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor.
Jun Lan,Jiwan Ge,Jinfang Yu,Sisi Shan,Huan Zhou,Shilong Fan,Qi Zhang,Xuanling Shi,Qisheng Wang,Linqi Zhang,Xinquan Wang +10 more
TLDR
High-resolution crystal structures of the receptor-binding domain of the spike protein of SARS-CoV-2 and SARS -CoV in complex with ACE2 provide insights into the binding mode of these coronaviruses and highlight essential ACE2-interacting residues.Abstract:
A new and highly pathogenic coronavirus (severe acute respiratory syndrome coronavirus-2, SARS-CoV-2) caused an outbreak in Wuhan city, Hubei province, China, starting from December 2019 that quickly spread nationwide and to other countries around the world1–3. Here, to better understand the initial step of infection at an atomic level, we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 bound to the cell receptor ACE2. The overall ACE2-binding mode of the SARS-CoV-2 RBD is nearly identical to that of the SARS-CoV RBD, which also uses ACE2 as the cell receptor4. Structural analysis identified residues in the SARS-CoV-2 RBD that are essential for ACE2 binding, the majority of which either are highly conserved or share similar side chain properties with those in the SARS-CoV RBD. Such similarity in structure and sequence strongly indicate convergent evolution between the SARS-CoV-2 and SARS-CoV RBDs for improved binding to ACE2, although SARS-CoV-2 does not cluster within SARS and SARS-related coronaviruses1–3,5. The epitopes of two SARS-CoV antibodies that target the RBD are also analysed for binding to the SARS-CoV-2 RBD, providing insights into the future identification of cross-reactive antibodies. High-resolution crystal structures of the receptor-binding domain of the spike protein of SARS-CoV-2 and SARS-CoV in complex with ACE2 provide insights into the binding mode of these coronaviruses and highlight essential ACE2-interacting residues.read more
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The Global Phosphorylation Landscape of SARS-CoV-2 Infection.
Mehdi Bouhaddou,Danish Memon,Bjoern Meyer,Kris M. White,Veronica V. Rezelj,Miguel Correa Marrero,Benjamin J. Polacco,James E. Melnyk,Svenja Ulferts,Robyn M. Kaake,Jyoti Batra,Alicia L. Richards,Erica Stevenson,David E. Gordon,Ajda Rojc,Kirsten Obernier,Jacqueline M. Fabius,Margaret Soucheray,Lisa Miorin,Elena Moreno,Cassandra Koh,Quang Dinh Tran,Alexandra Hardy,Rémy Robinot,Thomas Vallet,Benjamin E. Nilsson-Payant,Claudia Hernandez-Armenta,Alistair Dunham,Sebastian Weigang,Julian Knerr,Maya Modak,Diego Quintero,Yuan Zhou,Aurelien Dugourd,Alberto Valdeolivas,Trupti Patil,Qiongyu Li,Ruth Hüttenhain,Merve Cakir,Monita Muralidharan,Minkyu Kim,Gwendolyn M. Jang,Beril Tutuncuoglu,Joseph Hiatt,Jeffrey Z. Guo,Jiewei Xu,Sophia Bouhaddou,Christopher J.P. Mathy,Anna Gaulton,Emma J. Manners,Eloy Felix,Ying Shi,Marisa Goff,Jean K. Lim,Timothy McBride,Michael C. O’Neal,Yiming Cai,Jason C.J. Chang,David J. Broadhurst,Saker Klippsten,Emmie de Wit,Andrew R. Leach,Tanja Kortemme,Brian K. Shoichet,Melanie Ott,Julio Saez-Rodriguez,Benjamin R. tenOever,R. Dyche Mullins,Elizabeth R. Fischer,Georg Kochs,Robert Grosse,Adolfo García-Sastre,Marco Vignuzzi,Jeffery R. Johnson,Kevan M. Shokat,Danielle L. Swaney,Pedro Beltrao,Nevan J. Krogan +77 more
TL;DR: A quantitative mass spectrometry-based phosphoproteomics survey of SARS-CoV-2 infection in Vero E6 cells reveals dramatic rewiring of phosphorylation on host and viral proteins, revealing potential COVID-19 therapies.
Journal ArticleDOI
Insights into SARS-CoV-2 genome, structure, evolution, pathogenesis and therapies: Structural genomics approach.
Ahmad Abu Turab Naqvi,Kisa Fatima,Taj Mohammad,Urooj Fatima,Indrakant K. Singh,Archana Singh,Shaikh M. Atif,Gururao Hariprasad,Gulam Mustafa Hasan,Imtaiyaz Hassan +9 more
TL;DR: The analysis suggests a minimal variation in the genome sequence of SARS-CoV-2, may be responsible for a drastic change in the structures of target proteins, makes available drugs ineffective.
Journal ArticleDOI
SARS-CoV-2 Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses
Wanwisa Dejnirattisai,Jiandong Huo,D. Zhou,Jiří Zahradník,P Supasa,Changxiao Liu,Helen M. E. Duyvesteyn,Helen M. Ginn,Alexander J. Mentzer,Aekkachai Tuekprakhon,Rungtiwa Nutalai,Beibei Wang,Aiste Dijokaite,Suman Khan,Ori Avinoam,M.W. Bahar,Donal T. Skelly,S Adele,Síle A. Johnson,Thomas G Ritter,Chris Jb Mason,Christina Dold,Daniel Pan,Sara Assadi,A. Bellass,Nikki Omo-Dare,David Koeckerling,Amy Flaxman,D Jenkin,Parvinder K. Aley,Merryn Voysey,Sue Ann Costa Clemens,Felipe Gomes Naveca,Valdinete Alves do Nascimento,Fernanda Nascimento,Cristiano Fernandes da Costa,Paola Cristina Resende,Alex Pauvolid-Corrêa,Marilda M. Siqueira,Vicky L. Baillie,Natali Serafin,Gaurav Kwatra,Kelly Da Silva,Shabir A. Madhi,Marta C. Nunes,Tariq Mehmood Malik,Peter J. M. Openshaw,J Kenneth Baillie,Malcolm G Semple,Alain Townsend,Kuan-Ying A. Huang,Tiong Kit Tan,Miles W. Carroll,Paul Klenerman,Eleanor Barnes,Susanna Dunachie,Bede Constantinides,Hermione J. Webster,Derrick W. Crook,Andrew J. Pollard,Teresa Lambe,Neil G. Paterson,Mark Williams,Elizabeth E. Fry,Juthathip Mongkolsapaya,Jingshan Ren,Gideon Schreiber,David Stuart,Gavin R. Screaton +68 more
TL;DR: In this article , a new SARS-CoV-2 viral isolate Omicron-B.1.529 was announced, containing far more mutations in Spike (S) than previously reported variants, leading to a large number of mutations in the ACE2 binding site and rebalances receptor affinity to that of earlier pandemic viruses.
Journal ArticleDOI
CD147-spike protein is a novel route for SARS-CoV-2 infection to host cells.
Ke Wang,Wei Chen,Zheng Zhang,Yong-Qiang Deng,Jian-Qi Lian,Peng Du,Ding Wei,Yang Zhang,Xiu-Xuan Sun,Li Gong,Xu Yang,Lei He,Lei Zhang,Zhiwei Yang,Jie-Jie Geng,Ruo Chen,Zhang Hai,Bin Wang,Yu-Meng Zhu,Gang Nan,Jian-Li Jiang,Ling Li,Jiao Wu,Peng Lin,Wan Huang,Liangzhi Xie,Zhaohui Zheng,Kui Zhang,Jinlin Miao,Hong-Yong Cui,Min Huang,Jun Zhang,Ling Fu,Xiang-Min Yang,Zhongpeng Zhao,Shihui Sun,Hongjing Gu,Zhe Wang,Chun-Fu Wang,Yacheng Lu,Liu Yingying,Qing-Yi Wang,Huijie Bian,Ping Zhu,Zhi-Nan Chen +44 more
TL;DR: A novel virus entry route, CD147-spike protein, is revealed, which provides an important target for developing specific and effective drug against COVID-19.
Journal ArticleDOI
The Science Underlying COVID-19: Implications for the Cardiovascular System.
TL;DR: Persistent immune activation in predisposed patients, such as the elderly and those with CV risk, can lead to hemophagocytosis like syndrome, with uncontrolled amplification of cytokine production, leading to multi-organ failure and death.
References
More filters
Journal ArticleDOI
Clinical features of patients infected with 2019 novel coronavirus in Wuhan, China
Chaolin Huang,Yeming Wang,Xingwang Li,Lili Ren,Jianping Zhao,Yi Hu,Li Zhang,Guohui Fan,Jiuyang Xu,Xiaoying Gu,Zhenshun Cheng,Ting Yu,Jia'an Xia,Yuan Wei,Wenjuan Wu,Xuelei Xie,Wen Yin,Li Hui,Min Liu,Yan Xiao,Hong Gao,Li Guo,Jungang Xie,Guang-Fa Wang,Rongmeng Jiang,Zhancheng Gao,Qi Jin,Jianwei Wang,Bin Cao +28 more
TL;DR: The epidemiological, clinical, laboratory, and radiological characteristics and treatment and clinical outcomes of patients with laboratory-confirmed 2019-nCoV infection in Wuhan, China, were reported.
Journal ArticleDOI
Coot: model-building tools for molecular graphics.
Paul Emsley,Kevin Cowtan +1 more
TL;DR: CCP4mg is a project that aims to provide a general-purpose tool for structural biologists, providing tools for X-ray structure solution, structure comparison and analysis, and publication-quality graphics.
Journal ArticleDOI
A Novel Coronavirus from Patients with Pneumonia in China, 2019.
Na Zhu,Dingyu Zhang,Wenling Wang,Xingwang Li,Bo Yang,Jingdong Song,Xiang Zhao,Baoying Huang,Weifeng Shi,Roujian Lu,Peihua Niu,Faxian Zhan,Xuejun Ma,Dayan Wang,Wenbo Xu,Wenbo Xu,Guizhen Wu,George F. Gao,Wenjie Tan +18 more
TL;DR: Human airway epithelial cells were used to isolate a novel coronavirus, named 2019-nCoV, which formed a clade within the subgenus sarbecovirus, Orthocoronavirinae subfamily, which is the seventh member of the family of coronaviruses that infect humans.
Journal ArticleDOI
Phaser crystallographic software
Airlie J. McCoy,Ralf W. Grosse-Kunstleve,Paul D. Adams,Martyn Winn,Laurent C. Storoni,Randy J. Read +5 more
TL;DR: A description is given of Phaser-2.1: software for phasing macromolecular crystal structures by molecular replacement and single-wavelength anomalous dispersion phasing.
Journal ArticleDOI
A pneumonia outbreak associated with a new coronavirus of probable bat origin
Peng Zhou,Xing-Lou Yang,Xian Guang Wang,Ben Hu,Lei Zhang,Wei Zhang,Hao Rui Si,Yan Zhu,Bei Li,Chao Lin Huang,Hui-Dong Chen,Jing Chen,Yun Luo,Hua Guo,Ren Di Jiang,Meiqin Liu,Ying Chen,Xu Rui Shen,Xi Wang,Xiao Shuang Zheng,Kai Zhao,Quanjiao Chen,Fei Deng,Lin Lin Liu,Bing Yan,Fa Xian Zhan,Yan-Yi Wang,Gengfu Xiao,Zhengli Shi +28 more
TL;DR: Identification and characterization of a new coronavirus (2019-nCoV), which caused an epidemic of acute respiratory syndrome in humans in Wuhan, China, and it is shown that this virus belongs to the species of SARSr-CoV, indicates that the virus is related to a bat coronav virus.
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