The Spike of SARS-CoV-2: Uniqueness and Applications
Tóm tắt
Từ khóa
Tài liệu tham khảo
Drexler, 2014, Ecology, Evolution and Classification of Bat Coronaviruses in the Aftermath of SARS, Antiviral Res, 101, 45, 10.1016/j.antiviral.2013.10.013
Wu, 2020, A New Coronavirus Associated With Human Respiratory Disease in China, Nature, 579, 10.1038/s41586-020-2008-3
Zhou, 2020, A Pneumonia Outbreak Associated With a New Coronavirus of Probable Bat Origin, Nature, 579, 10.1038/s41586-020-2012-7
Lu, 2020, Genomic Characterisation and Epidemiology of 2019 Novel Coronavirus: Implications for Virus Origins and Receptor Binding, Lancet, 395, 10.1016/s0140-6736(20)30251-8
Vellingiri, 2020, COVID-19: A Promising Cure for the Global Panic, Sci Total Environ, 725, 10.1016/j.scitotenv.2020.138277
Wrapp, 2020, Cryo-EM Structure of the 2019-Ncov Spike in the Prefusion Conformation, Science, 367, 10.1126/science.abb2507
Li, 2016, Structure, Function, and Evolution of Coronavirus Spike Proteins, Annu Rev Virol, 3, 10.1146/annurev-virology-110615-042301
Wu, 2020, Genome Composition and Divergence of the Novel Coronavirus (2019-Ncov) Originating in China, Cell Host Microbe, 27, 10.1016/j.chom.2020.02.001
Jaimes, 2020, Phylogenetic Analysis and Structural Modeling of SARS-CoV-2 Spike Protein Reveals an Evolutionary Distinct and Proteolytically Sensitive Activation Loop, J Mol Biol, 432, 10.1016/j.jmb.2020.04.009
Ou, 2020, Characterization of Spike Glycoprotein of SARS-CoV-2 on Virus Entry and Its Immune Cross-Reactivity With SARS-CoV, Nat Commun, 11, 10.1038/s41467-020-15562-9
Li, 2015, Receptor Recognition Mechanisms of Coronaviruses: A Decade of Structural Studies, J Virol, 89, 10.1128/jvi.02615-14
Li, 2003, Angiotensin-Converting Enzyme 2 Is a Functional Receptor for the SARS Coronavirus, Nature, 426, 10.1038/nature02145
Du, 2013, Identification of a Receptor-Binding Domain in the S Protein of the Novel Human Coronavirus Middle East Respiratory Syndrome Coronavirus as an Essential Target for Vaccine Development, J Virol, 87, 10.1128/jvi.01048-13
Mou, 2013, The Receptor Binding Domain of the New Middle East Respiratory Syndrome Coronavirus Maps to a 231-Residue Region in the Spike Protein That Efficiently Elicits Neutralizing Antibodies, J Virol, 87, 10.1128/jvi.01277-13
Raj, 2013, Dipeptidyl Peptidase 4 Is a Functional Receptor for the Emerging Human Coronavirus-EMC, Nature, 495, 10.1038/nature12005
Jaimes, 2020, A Tale of Two Viruses: The Distinct Spike Glycoproteins of Feline Coronaviruses, Viruses, 12, 10.3390/v12010083
Lin, 2008, Identification of Residues in the Receptor-Binding Domain (RBD) of the Spike Protein of Human Coronavirus NL63 That Are Critical for the RBD–ACE2 Receptor Interaction, J Gen Virol, 89, 10.1099/vir.0.83331-0
Peng, 2012, Crystal Structure of Bovine Coronavirus Spike Protein Lectin Domain, J Biol Chem, 287, 10.1074/jbc.M112.418210
Promkuntod, 2014, Mapping of the Receptor-Binding Domain and Amino Acids Critical for Attachment in the Spike Protein of Avian Coronavirus Infectious Bronchitis Virus, Virology, 448, 26, 10.1016/j.virol.2013.09.018
Wang, 2019, Structural Definition of a Neutralization-Sensitive Epitope on the MERS-CoV S1-NTD, Cell Rep, 28, 3395, 10.1016/j.celrep.2019.08.052
Wang, 2020, Structural and Functional Basis of SARS-CoV-2 Entry by Using Human Ace2, Cell, 181, 894, 10.1016/j.cell.2020.03.045
Millet, 2015, Host Cell Proteases: Critical Determinants of Coronavirus Tropism and Pathogenesis, Virus Res, 202, 10.1016/j.virusres.2014.11.021
Coutard, 2020, The Spike Glycoprotein of the New Coronavirus 2019-Ncov Contains a Furin-Like Cleavage Site Absent in CoV of the Same Clade, Antiviral Res, 176, 10.1016/j.antiviral.2020.104742
Follis, 2006, Furin Cleavage of the SARS Coronavirus Spike Glycoprotein Enhances Cell–Cell Fusion But Does Not Affect Virion Entry, Virology, 350, 10.1016/j.virol.2006.02.003
Belouzard, 2009, Activation of the SARS Coronavirus Spike Protein via Sequential Proteolytic Cleavage at Two Distinct Sites, Proc Natl Acad Sci, 106, 10.1073/pnas.0809524106
Yan, 2018, Crystal Structure of the Post-Fusion Core of the Human Coronavirus 229E Spike Protein at 1.86 Å Resolution, Acta Crystallogr Section D Struct Biol, 74, 10.1107/s2059798318008318
Kumar, 2020, Structural, Glycosylation and Antigenic Variation Between 2019 Novel Coronavirus (2019-Ncov) and SARS Coronavirus (SARS-CoV), VirusDisease, 31, 13, 10.1007/s13337-020-00571-5
Mycroft-West, 2020, The 2019 Coronavirus (SARS-CoV-2) Surface Protein (Spike) S1 Receptor Binding Domain Undergoes Conformational Change Upon Heparin Binding, bioRxiv, 10.1101/2020.02.29.971093
Sun, 2020, SARS-CoV-2 and SARS-CoV Spike-RBD Structure and Receptor Binding Comparison and Potential Implications on Neutralizing Antibody and Vaccine Development, bioRxiv, 10.1101/2020.02.16.951723
Walls, 2020, Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein, Cell, 181, 281, 10.1016/j.cell.2020.02.058
Hoffmann, 2020, Pöhlmann S. A Multibasic Cleavage Site in the Spike Protein of SARS-CoV-2 Is Essential for Infection of Human Lung Cells, Mol Cell, 78, 779, 10.1016/j.molcel.2020.04.022
Li, 2008, T Cell Responses to Whole SARS Coronavirus in Humans, J Immunol, 181, 10.4049/jimmunol.181.8.5490
Prompetchara, 2020, Immune Responses in COVID-19 and Potential Vaccines: Lessons Learned From SARS and MERS Epidemic, Asian Pac J Allergy Immunol, 38, 1, 10.12932/ap-200220-0772
Brielle, 2020, The SARS-CoV-2 Exerts a Distinctive Strategy for Interacting With the ACE2 Human Receptor, bioRxiv, 10.1101/2020.03.10.986398
Wec, 2020, Broad Sarbecovirus Neutralizing Antibodies Define a Key Site of Vulnerability on the SARS-CoV-2 Spike Protein, bioRxiv, 10.1101/2020.05.15.096511
Hoffmann, 2020, SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor, Cell, 181, 271, 10.1016/j.cell.2020.02.052
Chen, 2020, Potential for Developing a SARS-CoV Receptor-Binding Domain (RBD) Recombinant Protein as a Heterologous Human Vaccine Against Coronavirus Infectious Disease (COVID)-19, Hum Vaccines Immunother, 16, 10.1080/21645515.2020.1740560
Robson, 2020, COVID-19 Coronavirus Spike Protein Analysis for Synthetic Vaccines, a Peptidomimetic Antagonist, and Therapeutic Drugs, and Analysis of a Proposed Achilles’ Heel Conserved Region to Minimize Probability of Escape Mutations and Drug Resistance, Comput Biol Med, 121, 10.1016/j.compbiomed.2020.103749
Uddin, 2020, Ancestral Origin, Antigenic Resemblance and Epidemiological Insights of Novel Coronavirus (SARS-CoV-2): Global Burden and Bangladesh Perspective, Infect Genet Evol, 84, 104440, 10.1016/j.meegid.2020.104440
Wahba, 2020, Identification of a Pangolin Niche for a 2019-Ncov-Like Coronavirus Through an Extensive Meta-Metagenomic Search, mSphere, 5, 10.1101/2020.02.08.939660
Wong, 2020, Evidence of Recombination in Coronaviruses Implicating Pangolin Origins of Ncov-2019, bioRxiv, 10.1101/2020.02.07.939207
Xiao, 2020, Isolation of SARS-CoV-2-Related Coronavirus From Malayan Pangolins, Nature, 583, 10.1038/s41586-020-2313-x
Zhang, 2020, Protein Structure and Sequence Reanalysis of 2019-Ncov Genome Refutes Snakes as Its Intermediate Host and the Unique Similarity Between Its Spike Protein Insertions and HIV-1, J Proteome Res, 19, 10.1021/acs.jproteome.0c00129
Guo, 2020, Evolutionary Arms Race Between Virus and Host Drives Genetic Diversity in Bat Severe Acute Respiratory Syndrome-Related Coronavirus Spike Genes, J Virol, 94, 10.1128/jvi.00902-20
Jackwood, 2010, Emergence of a Group 3 Coronavirus Through Recombination, Virology, 398, 98, 10.1016/j.virol.2009.11.044
Perlman, 2020, Are Pangolins the Intermediate Host of the 2019 Novel Coronavirus (SARS-CoV-2), PloS Pathog, 16, 10.1371/journal.ppat.1008421
Ou, 2020, Emergence of SARS-CoV-2 Spike RBD Mutants That Enhance Viral Infectivity Through Increased Human ACE2 Receptor Binding Affinity, bioRxiv, 10.1101/2020.03.15.991844
Chen, 2020, Mutations Strengthened SARS-CoV-2 Infectivity, J Mol Biol, 432, 10.1016/j.jmb.2020.07.009
Peng, 2020, Exploring the Binding Mechanism and Accessible Angle of SARS-CoV-2 Spike and ACE2 by Molecular Dynamics Simulation and Free Energy Calculation, chemrxiv, 10.26434/chemrxiv.11877492.v1
Veeramachaneni, 2020, Structural and Simulation Analysis of Hotspot Residues Interactions of SARS-CoV 2 With Human ACE2 Receptor, J Biomolec Struct Dynam, 39, 10.1080/07391102.2020.1773318
Vankadari, 2020, Emerging COVID-19 Coronavirus: Glycan Shield and Structure Prediction of Spike Glycoprotein and Its Interaction With Human CD26, Emerg Microbes Infect, 9, 10.1080/22221751.2020.1739565
Vankadari, 2020, Arbidol: A Potential Antiviral Drug for the Treatment of SARS-CoV-2 by Blocking Trimerization of the Spike Glycoprotein, Int J Antimicrob Agents, 56, 105998, 10.1016/j.ijantimicag.2020.105998
Lan, 2020, Structure of the SARS-CoV-2 Spike Receptor-Binding Domain Bound to the ACE2 Receptor, Nature, 581, 10.1038/s41586-020-2180-5
Xia, 2020, The Role of Furin Cleavage Site in SARS-CoV-2 Spike Protein-Mediated Membrane Fusion in the Presence or Absence of Trypsin, Signal Transduct Target Ther, 5, 92, 10.1038/s41392-020-0184-0
Ali, 2020, Dynamics of the ACE2–SARS-CoV-2/SARS-CoV Spike Protein Interface Reveal Unique Mechanisms, Sci Rep, 10, 14214, 10.1038/s41598-020-71188-3
Schuster, 2021, Specific and Rapid SARS-CoV-2 Identification Based on LC-MS/MS Analysis, ACS Omega, 6, 10.1021/acsomega.0c04691
Wang, 2020, CD147-Spike Protein Is a Novel Route for SARS-CoV-2 Infection to Host Cells, Signal Transduct Target Ther, 5, 283, 10.1038/s41392-020-00426-x
Cava, 2020, In Silico Discovery of Candidate Drugs Against Covid-19, Viruses, 12, 404, 10.3390/v12040404
Hoffmann, 2018, Priming Time: How Cellular Proteases Arm Coronavirus Spike Proteins, Activation of Viruses by Host Proteases, 71, 10.1007/978-3-319-75474-1_4
Steinhauer, 1999, Role of Hemagglutinin Cleavage for the Pathogenicity of Influenza, Virus Virol, 258, 1, 10.1006/viro.1999.9716
Wang, 2020, Lectin-Like Intestinal Defensin Inhibits 2019-Ncov Spike Binding to ACE2, bioRxiv, 10.1101/2020.03.29.013490
Shang, 2020, Structural Basis of Receptor Recognition by SARS-CoV-2, Nature, 581, 10.1038/s41586-020-2179-y
Whisenant, 2020, Blocking Coronavirus 19 Infection via the SARS-CoV-2 Spike Protein: Initial Steps, ACS Med Chem Lett, 11, 10.1021/acsmedchemlett.0c00233
Zhang, 2020, The First-in-Class Peptide Binder to the SARS-CoV-2 Spike Protein, bioRxiv, 10.1101/2020.03.19.999318
Barh, 2020, Potential Chimeric Peptides to Block the SARS-CoV-2 Spike Receptor-Binding Domain, F1000Research, 9, 576, 10.12688/f1000research.24074.1
Cantuti-Castelvetri, 2020, Neuropilin-1 Facilitates SARS-CoV-2 Cell Entry and Infectivity, Science, 370, 10.1126/science.abd2985
Davies, 2020, Neuropilin1 as a New Potential SARSCoV2 Infection Mediator Implicated in the Neurologic Features and Central Nervous System Involvement of COVID19, Mol Med Rep, 22, 10.3892/mmr.2020.11510
Kerslake, 2020, Coexpression of Peripheral Olfactory Receptors With SARSCoV2 Infection Mediators: Potential Implications Beyond Loss of Smell as a COVID19 Symptom, Int J Mol Med, 46, 10.3892/ijmm.2020.4646
Zamorano Cuervo, 2020, ACE2: Evidence of Role as Entry Receptor for SARS-CoV-2 and Implications in Comorbidities, Elife, 9, e61390, 10.7554/eLife.61390
Cui, 2020, AGTR2, One Possible Novel Key Gene for the Entry of SARS-CoV-2 Into Human Cells, IEEE/ACM Trans Comput Biol Bioinform, 10.1109/TCBB.2020.3009099
Gordon, 2020, A SARS-CoV-2-Human Protein-Protein Interaction Map Reveals Drug Targets and Potential Drug-Repurposing, bioRxiv, 10.1101/2020.03.22.002386
Ningombam, 2021, Mutant Strains of SARS-CoV-2 Are More Prone to Infect Obese Patient: A Review, Wien Klin Wochenschr, 133, 10.1007/s00508-021-01819-w
Rani, 2021, Symptomatic Reinfection of SARS-CoV-2 With Spike Protein Variant N440K Associated With Immune Escape, J Med Virol, 93, 10.1002/jmv.26997
Bayarri-Olmos, 2021, The SARS-CoV-2 Y453F Mink Variant Displays a Pronounced Increase in ACE-2 Affinity But Does Not Challenge Antibody Neutralization, J Biol Chem, 296, 100536, 10.1016/j.jbc.2021.100536
Rambaut, 2020, A Dynamic Nomenclature Proposal for SARS-CoV-2 Lineages to Assist Genomic Epidemiology, Nat Microbiol, 5, 10.1038/s41564-020-0770-5
Gomez, 2021, Emerging SARS-CoV-2 Variants and Impact in Global Vaccination Programs Against SARS-CoV-2/COVID-19, Vaccines (Basel), 9, 243, 10.3390/vaccines9030243
Hossain, 2021, The Emergence of New Strains of SARS-CoV-2. What Does It Mean for COVID-19 Vaccines, Expert Rev Vaccines, 1, 10.1080/14760584.2021.1915140
Greinacher, 2021, Thrombotic Thrombocytopenia After ChAdOx1 Ncov-19 Vaccination, N Engl J Med, 384, 10.1056/NEJMoa2104840
Ostergaard, 2021, Thromboembolism and the Oxford-AstraZeneca COVID-19 Vaccine: Side-Effect or Coincidence, Lancet, 397, 10.1016/S0140-6736(21)00762-5
MacNeil, 2021, Updated Recommendations From the Advisory Committee on Immunization Practices for Use of the Janssen (Johnson & Johnson) COVID-19 Vaccine After Reports of Thrombosis With Thrombocytopenia Syndrome Among Vaccine Recipients - United States, April 2021, MMWR Morb Mortal Wkly Rep, 70, 10.15585/mmwr.mm7017e4
McBride, 2014, The Coronavirus Nucleocapsid Is a Multifunctional, Protein Viruses, 6, 2991, 10.3390/v6082991
Li, 2020, Molecular Immune Pathogenesis and Diagnosis of COVID-19, J Pharm Anal, 10, 10.1016/j.jpha.2020.03.001
Jaeger, 2021, Adjusting RT-qPCR Conditions to Avoid Unspecific Amplification in SARS-CoV-2 Diagnosis, Int J Infect Dis, 102, 10.1016/j.ijid.2020.10.079
Won, 2020, Development of a Laboratory-Safe and Low-Cost Detection Protocol for SARS-CoV-2 of the Coronavirus Disease 2019 (COVID-19), Exp Neurobiol, 29, 10.5607/en20009
To, 2020, Consistent Detection of 2019 Novel Coronavirus in Saliva, Clin Infect Dis, 71, 10.1093/cid/ciaa149
Xu, 2020, High Expression of ACE2 Receptor of 2019-Ncov on the Epithelial Cells of Oral Mucosa, Int J Oral Sci, 12, 8, 10.1038/s41368-020-0074-x
Xu, 2020, Saliva: Potential Diagnostic Value and Transmission of 2019-Ncov, Int J Oral Sci, 12, 11, 10.1038/s41368-020-0080-z
Teo, 2021, Saliva Is More Sensitive Than Nasopharyngeal or Nasal Swabs for Diagnosis of Asymptomatic and Mild COVID-19 Infection, Sci Rep, 11, 3134, 10.1038/s41598-021-82787-z
Ramirez, 2021, Will the Emergent SARS-CoV2 B.1.1.7 Lineage Affect Molecular Diagnosis of COVID-19, J Med Virol, 93, 10.1002/jmv.26823
Jain, 2021, Analysis of the Potential Impact of Genomic Variants in Global SARS-CoV-2 Genomes on Molecular Diagnostic Assays, Int J Infect Dis, 102, 10.1016/j.ijid.2020.10.086
Li, 2020, Development and Clinical Application of a Rapid IgM-IgG Combined Antibody Test for SARS-CoV-2 Infection Diagnosis, J Med Virol, 92, 10.1002/jmv.25727
Racine, 2009, IgM in Microbial Infections: Taken for Granted, Immunol Lett, 125, 79, 10.1016/j.imlet.2009.06.003
Harrington, 2021, Rapid Decline of Neutralizing Antibodies Is Associated With Decay of IgM in Adults Recovered From Mild COVID-19, Cell Rep Med, 2, 10.1016/j.xcrm.2021.100253
Al-Jighefee, 2021, Evaluation of Antibody Response in Symptomatic and Asymptomatic COVID-19 Patients and Diagnostic Assessment of New IgM/IgG ELISA Kits, Pathogens, 10, 161, 10.3390/pathogens10020161
Liu, 2020, Evaluation of Nucleocapsid and Spike Protein-Based Enzyme-Linked Immunosorbent Assays for Detecting Antibodies Against SARS-CoV-2, J Clin Microbiol, 58, 10.1128/jcm.00461-20
Seo, 2020, Rapid Detection of COVID-19 Causative Virus (SARS-CoV-2) in Human Nasopharyngeal Swab Specimens Using Field-Effect Transistor-Based Biosensor, ACS Nano, 14, 10.1021/acsnano.0c02823
Barlev-Gross, 2021, Spike vs Nucleocapsid SARS-CoV-2 Antigen Detection: Application in Nasopharyngeal Swab Specimens, Anal Bioanal Chem, 413, 10.1007/s00216-021-03298-4
Lee, 2021, A Novel Rapid Detection for SARS-CoV-2 Spike 1 Antigens Using Human Angiotensin Converting Enzyme 2 (ACE2), Biosens Bioelectron, 171, 10.1016/j.bios.2020.112715
Yakoh, 2021, Paper-Based Electrochemical Biosensor for Diagnosing COVID-19: Detection of SARS-CoV-2 Antibodies and Antigen, Biosens Bioelectron, 176, 10.1016/j.bios.2020.112912
Rockx, 2008, Structural Basis for Potent Cross-Neutralizing Human Monoclonal Antibody Protection Against Lethal Human and Zoonotic Severe Acute Respiratory Syndrome Coronavirus Challenge, J Virol, 82, 10.1128/jvi.02377-07
Coughlin, 2009, Human Monoclonal Antibodies to SARS-Coronavirus Inhibit Infection by Different Mechanisms, Virology, 394, 39, 10.1016/j.virol.2009.07.028
Ohnuma, 2013, Inhibition of Middle East Respiratory Syndrome Coronavirus Infection by Anti-CD26 Monoclonal Antibody, J Virol, 87, 10.1128/jvi.02448-13
Lei, 2020, Neutralization of SARS-CoV-2 Spike Pseudotyped Virus by Recombinant ACE2-Ig, Nat Commun, 11, 2070, 10.1038/s41467-020-16048-4
Chen, 2020, Human Monoclonal Antibodies Block the Binding of SARS-CoV-2 Spike Protein to Angiotensin Converting Enzyme 2 Receptor, Cell Mol Immunol, 17, 10.1038/s41423-020-0426-7
Millet, 2016, Middle East Respiratory Syndrome Coronavirus Infection Is Inhibited by Griffithsin, Antiviral Res, 133, 1, 10.1016/j.antiviral.2016.07.011
Amin, 2020, Docking Study of Chloroquine and Hydroxychloroquine Interaction With RNA Binding Domain of Nucleocapsid Phospho-Protein – An in Silico Insight Into the Comparative Efficacy of Repurposing Antiviral Drugs, J Biomolec Struct Dynam, 2020, 1, 10.1080/07391102.2020.1775703
Wei, 2020, In Silico Screening of Potential Spike Glycoprotein Inhibitors of SARS-CoV-2 With Drug Repurposing Strategy, Res Sq, 10.21203/rs.3.rs-17720/v1
Du, 2009, The Spike Protein of SARS-CoV — A Target for Vaccine and Therapeutic Development, Nat Rev Microbiol, 7, 10.1038/nrmicro2090
Zhang, 2014, Current Advancements and Potential Strategies in the Development of MERS-CoV Vaccines, Expert Rev Vaccines, 13, 10.1586/14760584.2014.912134
Yuan, 2020, A Highly Conserved Cryptic Epitope in the Receptor Binding Domains of SARS-CoV-2 and SARS-CoV, Science, 368, 10.1126/science.abb7269
Robson, 2020, Computers and Viral Diseases. Preliminary Bioinformatics Studies on the Design of a Synthetic Vaccine and a Preventative Peptidomimetic Antagonist Against the SARS-CoV-2 (2019-Ncov, COVID-19) Coronavirus, Comput Biol Med, 119, 103670, 10.1016/j.compbiomed.2020.103670
Bisht, 2004, Severe Acute Respiratory Syndrome Coronavirus Spike Protein Expressed by Attenuated Vaccinia Virus Protectively Immunizes Mice, Proc Natl Acad Sci, 101, 10.1073/pnas.0401939101
Yang, 2004, A DNA Vaccine Induces SARS Coronavirus Neutralization and Protective Immunity in Mice, Nature, 428, 10.1038/nature02463
He, 2006, Cross-Neutralization of Human and Palm Civet Severe Acute Respiratory Syndrome Coronaviruses by Antibodies Targeting the Receptor-Binding Domain of Spike Protein, J Immunol, 176, 10.4049/jimmunol.176.10.6085
Yu, 2005, Production of a Monoclonal Antibody Against SARS-CoV Spike Protein With Single Intrasplenic Immunization of Plasmid DNA, Immunol Lett, 100, 10.1016/j.imlet.2005.03.015
Spitz, 1984, Intrasplenic Primary Immunization for the Production of Monoclonal Antibodies, J Immunol Methods, 70, 39, 10.1016/0022-1759(84)90387-9
Liu, 2006, Production of an Anti-Severe Acute Respiratory Syndrome (SARS) Coronavirus Human Monoclonal Antibody Fab Fragment by Using a Combinatorial Immunoglobulin Gene Library Derived From Patients Who Recovered From SARS, Clin Vaccine Immunol, 13, 10.1128/cvi.13.5.594-597.2006
Wu, 2020, An Alternative Binding Mode of IGHV3-53 Antibodies to the SARS-CoV-2 Receptor Binding Domain, Cell Rep, 33, 10.1016/j.celrep.2020.108274
Ling, 2020, In Silico Design of Antiviral Peptides Targeting the Spike Protein of SARS-CoV-2, Peptides, 130, 170328, 10.1016/j.peptides.2020.170328
Lu, 2014, Structure-Based Discovery of Middle East Respiratory Syndrome Coronavirus Fusion Inhibitor, Nat Commun, 5, 3067, 10.1038/ncomms4067
Qian, 2013, Role of the Spike Glycoprotein of Human Middle East Respiratory Syndrome Coronavirus (MERS-CoV) in Virus Entry and Syncytia Formation, PloS One, 8, 10.1371/journal.pone.0076469
Millet, 2014, Host Cell Entry of Middle East Respiratory Syndrome Coronavirus After Two-Step, Furin-Mediated Activation of the Spike Protein, Proc Natl Acad Sci, 111, 10.1073/pnas.1407087111
Du, 2016, MERS-CoV Spike Protein: A Key Target for Antivirals, Expert Opin Ther Targets, 21, 10.1080/14728222.2017.1271415
Silva Andrade, 2020, Computational Screening for Potential Drug Candidates Against the SARS-CoV-2 Main Protease, F1000Research, 9, 514, 10.12688/f1000research.23829.1
Han, 2020, Identification of Candidate COVID-19 Therapeutics Using hPSC-Derived Lung Organoids, bioRxiv, 10.1101/2020.05.05.079095
Xiong, 2020, Several FDA-Approved Drugs Effectively Inhibit SARS-CoV-2 Infection In Vitro, bioRxiv, 10.1101/2020.06.05.135996
Thanh Le, 2020, The COVID-19 Vaccine Development Landscape, Nat Rev Drug Discov, 19, 10.1038/d41573-020-00073-5
Dhama, 2020, COVID-19, an Emerging Coronavirus Infection: Advances and Prospects in Designing and Developing Vaccines, Immunotherapeutics, and Therapeutics, Hum Vaccines Immunother, 16, 10.1080/21645515.2020.1735227
Myung Hee Kim, 2019, Jun Chang. Superior Immune Responses Induced by Intranasal Immunization With Recombinant Adenovirus-Based Vaccine Expressing Full-Length Spike Protein of Middle East Respiratory Syndrome Coronavirus, PloS One, 14, e0220196, 10.1371/journal.pone.0220196
Liu, 2017, T-Cell Immunity of SARS-CoV: Implications for Vaccine Development Against MERS-CoV, Antiviral Res, 137, 82, 10.1016/j.antiviral.2016.11.006
Giurgea, 2020, Universal Coronavirus Vaccines: The Time to Start Is Now, NPJ Vaccines, 5, 43, 10.1038/s41541-020-0198-1
Grifoni, 2020, Targets of T Cell Responses to SARS-CoV-2 Coronavirus in Humans With COVID-19 Disease and Unexposed Individuals, Cell, 181, 1489, 10.1016/j.cell.2020.05.015
Le Bert, 2020, SARS-CoV-2-Specific T Cell Immunity in Cases of COVID-19 and SARS, and Uninfected Controls, Nature, 584, 10.1038/s41586-020-2550-z
Mateus, 2020, Selective and Cross-Reactive SARS-CoV-2 T Cell Epitopes in Unexposed Humans, Science, 370, 89, 10.1126/science.abd3871
Cohen, 2021, Neutralizing and Cross-Reacting Antibodies: Implications for Immunotherapy and SARS-CoV-2 Vaccine Development, Hum Vaccines Immunother, 17, 84, 10.1080/21645515.2020.1787074
Lv, 2020, Cross-Reactive Antibody Response Between SARS-CoV-2 and SARS-CoV Infections, Cell Rep, 31, 107725, 10.1016/j.celrep.2020.107725
Wan, 2020, Cross-Reaction of Sera From COVID-19 Patients With SARS-CoV Assays, medRxiv, 10.1101/2020.03.17.20034454
Chagla, 2021, In High-Risk Adults, the Moderna Vaccine had 94% Efficacy Against COVID-19 >/=14 D After the 2nd Dose, Ann Intern Med, 174, JC28, 10.7326/ACPJ202103160-028
Abu-Raddad, 2021, Effectiveness of the BNT162b2 Covid-19 Vaccine Against the B.1.1.7 and B.1.351 Variants, N Engl J Med, NEJMc2104974, 10.1056/NEJMc2104974
Livingston, 2021, The Johnson & Johnson Vaccine for COVID-19, JAMA, 325, 1575, 10.1001/jama.2021.2927
Sadoff, 2021, Interim Results of a Phase 1–2a Trial of Ad26.COV2.S Covid-19 Vaccine, New Engl J Med, 384, 10.1056/NEJMoa2034201
Baden, 2021, Efficacy and Safety of the mRNA-1273 SARS-CoV-2 Vaccine, N Engl J Med, 384, 10.1056/NEJMoa2035389
Knoll, 2021, Oxford-AstraZeneca COVID-19 Vaccine Efficacy, Lancet, 397, 10.1016/S0140-6736(20)32623-4
Jones, 2021, Sputnik V COVID-19 Vaccine Candidate Appears Safe and Effective, Lancet, 397, 10.1016/S0140-6736(21)00191-4
Baraniuk, 2021, Covid-19: What Do We Know About Sputnik V and Other Russian Vaccines, BMJ, 372, n743, 10.1136/bmj.n743
Kumar, 2021, Status Report on COVID-19 Vaccines Development, Curr Infect Dis Rep, 23, 9, 10.1007/s11908-021-00752-3
Kumar, 2021, An Evolutionary Portrait of the Progenitor SARS-CoV-2 and Its Dominant Offshoots in COVID-19 Pandemic, Mol Biol Evol, msab118, 10.1093/molbev/msab118