Virological characteristics of the SARS-CoV-2 Omicron BA.2.75 variant
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J. Zahradník | G. Schreiber | H. Nasser | Kazuo Takayama | H. Sawa | T. Fukuhara | Tomokazu Tamura | K. Matsuno | M. Tsuda | Naganori Nao | Jumpei Ito | A. Takaori-Kondo | K. Yoshimatsu | T. Irie | K. Maenaka | Akatsuki Saito | K. Sasaki-Tabata | S. Kita | H. Fukuhara | T. Hashiguchi | K. Sadamasu | T. Ueno | K. Yoshimura | I. Kimura | Y. Kosugi | Daichi Yamasoba | K. Uriu | Lei Wang | Sayaka Deguchi | Terumasa Ikeda | J. Kuramochi | Kayoko Nagata | Koshiro Tabata | Tetsuharu Nagamoto | M. Nagashima | Mako Toyoda | Yuki Anraku | Kei Sato | Shinya Tanaka | Ryo Shimizu | H. Ito | Yoshitaka Oda | Hiroyuki Asakura | Shigeru Fujita | M. Shofa | Y. Yamamoto | M.S.T. Monira Begum | R. Suzuki | Jin Kuramochi | T. Nagamoto | Keita Matsuno | K. Takayama | A. Takaori‐Kondo
[1] D. Montefiori,et al. Neutralization of SARS-CoV-2 Omicron BA.2.75 after mRNA-1273 Vaccination , 2022, The New England journal of medicine.
[2] H. Date,et al. SARS-CoV-2 disrupts respiratory vascular barriers by suppressing Claudin-5 expression , 2022, Science advances.
[3] Fei Shao,et al. Characterizations of enhanced infectivity and antibody evasion of Omicron BA.2.75 , 2022, bioRxiv.
[4] J. Zahradník,et al. Virological characteristics of the SARS-CoV-2 Omicron BA.2.75 , 2022, bioRxiv.
[5] Y. Ohba,et al. Comparative pathogenicity of SARS-CoV-2 Omicron subvariants including BA.1, BA.2, and BA.5 , 2022, bioRxiv.
[6] J. P. Almeida,et al. SARS-CoV-2 BA.5 vaccine breakthrough risk and severity compared with BA.2: a case-case and cohort study using Electronic Health Records in Portugal , 2022, medRxiv.
[7] Qian Wang,et al. Antibody evasion by SARS-CoV-2 Omicron subvariants BA.2.12.1, BA.4 and BA.5 , 2022, Nature.
[8] P. Schommers,et al. SARS-CoV-2 Omicron sublineages exhibit distinct antibody escape patterns , 2022, Cell Host & Microbe.
[9] D. Barouch,et al. Neutralization Escape by SARS-CoV-2 Omicron Subvariants BA.2.12.1, BA.4, and BA.5 , 2022, The New England journal of medicine.
[10] G. Lozanski,et al. Neutralization of the SARS-CoV-2 Omicron BA.4/5 and BA.2.12.1 Subvariants , 2022, The New England journal of medicine.
[11] Fei Shao,et al. BA.2.12.1, BA.4 and BA.5 escape antibodies elicited by Omicron infection , 2022, Nature.
[12] Jumpei Ito,et al. Neutralisation sensitivity of SARS-CoV-2 omicron subvariants to therapeutic monoclonal antibodies , 2022, The Lancet Infectious Diseases.
[13] P. Klenerman,et al. Antibody escape of SARS-CoV-2 Omicron BA.4 and BA.5 from vaccine and BA.1 serum , 2022, Cell.
[14] Diane J Post,et al. Rapid decline in vaccine-boosted neutralizing antibodies against SARS-CoV-2 Omicron variant , 2022, Cell Reports Medicine.
[15] H. Jäck,et al. Augmented neutralisation resistance of emerging omicron subvariants BA.2.12.1, BA.4, and BA.5 , 2022, The Lancet Infectious Diseases.
[16] Takeshi Noda,et al. Cell response analysis in SARS-CoV-2 infected bronchial organoids , 2022, Communications Biology.
[17] K. Ishii,et al. Virological characteristics of the SARS-CoV-2 Omicron BA.2 spike , 2022, Cell.
[18] A. Sigal,et al. Omicron sub-lineages BA.4/BA.5 escape BA.1 infection elicited neutralizing immunity , 2022, medRxiv.
[19] J. Zahradník,et al. The SARS-CoV-2 spike S375F mutation characterizes the Omicron BA.1 variant , 2022, bioRxiv.
[20] P. Maes,et al. Serum neutralization of SARS-CoV-2 Omicron sublineages BA.1 and BA.2 in patients receiving monoclonal antibodies , 2022, Nature Medicine.
[21] Shinji Watanabe,et al. Efficacy of Antiviral Agents against the SARS-CoV-2 Omicron Subvariant BA.2 , 2022, The New England journal of medicine.
[22] A. Takaori-Kondo,et al. Characterization of the immune resistance of SARS-CoV-2 Mu variant and the robust immunity induced by Mu infection , 2022, The Journal of infectious diseases.
[23] A. Kaneda,et al. Attenuated fusogenicity and pathogenicity of SARS-CoV-2 Omicron variant , 2022, Nature.
[24] A. Mittal,et al. Structural and antigenic variations in the spike protein of emerging SARS-CoV-2 variants , 2022, PLoS pathogens.
[25] Shinji Watanabe,et al. Efficacy of Antibodies and Antiviral Drugs against Covid-19 Omicron Variant , 2022, The New England journal of medicine.
[26] S. Madhi,et al. SARS-CoV-2 Omicron-B.1.1.529 leads to widespread escape from neutralizing antibody responses , 2022, Cell.
[27] D. Fremont,et al. An infectious SARS-CoV-2 B.1.1.529 Omicron virus escapes neutralization by therapeutic monoclonal antibodies , 2021, Research square.
[28] T. Ndung’u,et al. Omicron extensively but incompletely escapes Pfizer BNT162b2 neutralization , 2021, Nature.
[29] P. Maes,et al. Considerable escape of SARS-CoV-2 Omicron to antibody neutralization , 2021, Nature.
[30] Fei Shao,et al. Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies , 2021, Nature.
[31] Liyuan Liu,et al. Striking antibody evasion manifested by the Omicron variant of SARS-CoV-2 , 2021, Nature.
[32] S. Maurer-Stroh,et al. GISAID’s Role in Pandemic Response , 2021, China CDC weekly.
[33] J. Zahradník,et al. The SARS-CoV-2 Lambda variant exhibits enhanced infectivity and immune resistance , 2021, Cell Reports.
[34] Y. Kawaoka,et al. Enhanced fusogenicity and pathogenicity of SARS-CoV-2 Delta P681R mutation , 2021, Nature.
[35] Debabrata Dey,et al. A Protein-Engineered, Enhanced Yeast Display Platform for Rapid Evolution of Challenging Targets , 2021, ACS synthetic biology.
[36] A. Kaneda,et al. Neutralization of the SARS-CoV-2 Mu Variant by Convalescent and Vaccine Serum , 2021, The New England journal of medicine.
[37] M. Farzan,et al. Mechanisms of SARS-CoV-2 entry into cells , 2021, Nature reviews. Molecular cell biology.
[38] M. Diamond,et al. Genetic and structural basis for SARS-CoV-2 variant neutralization by a two-antibody cocktail , 2021, Nature Microbiology.
[39] D. Standley,et al. The SARS-CoV-2 Delta variant is poised to acquire complete resistance to wild-type spike vaccines , 2021, bioRxiv.
[40] O. Dym,et al. SARS-CoV-2 variant prediction and antiviral drug design are enabled by RBD in vitro evolution , 2021, Nature Microbiology.
[41] S. Ovchinnikov,et al. ColabFold: making protein folding accessible to all , 2022, Nature Methods.
[42] K. Maeda,et al. Usability of Polydimethylsiloxane-Based Microfluidic Devices in Pharmaceutical Research Using Human Hepatocytes. , 2021, ACS biomaterials science & engineering.
[43] Ravindra K. Gupta,et al. SARS-CoV-2 B.1.617 Mutations L452R and E484Q Are Not Synergistic for Antibody Evasion , 2021, The Journal of infectious diseases.
[44] J. Zahradník,et al. SARS-CoV-2 spike L452R variant evades cellular immunity and increases infectivity , 2021, Cell Host & Microbe.
[45] William T. Harvey,et al. SARS-CoV-2 variants, spike mutations and immune escape , 2021, Nature Reviews Microbiology.
[46] S. Lok. An NTD supersite of attack , 2021, Cell Host & Microbe.
[47] J. Dye,et al. LY-CoV1404 (bebtelovimab) potently neutralizes SARS-CoV-2 variants , 2021, bioRxiv.
[48] Ilya J. Finkelstein,et al. Prevalent, protective, and convergent IgG recognition of SARS-CoV-2 non-RBD spike epitopes , 2021, Science.
[49] A. Iafrate,et al. Multiple SARS-CoV-2 variants escape neutralization by vaccine-induced humoral immunity , 2021, Cell.
[50] S. Kishigami,et al. SARS-CoV-2 D614G spike mutation increases entry efficiency with enhanced ACE2-binding affinity , 2021, Nature Communications.
[51] Larissa B. Thackray,et al. Neutralizing and protective human monoclonal antibodies recognizing the N-terminal domain of the SARS-CoV-2 spike protein , 2021, Cell.
[52] M. Beltramello,et al. N-terminal domain antigenic mapping reveals a site of vulnerability for SARS-CoV-2 , 2021, bioRxiv.
[53] Jihun Lee,et al. A therapeutic neutralizing antibody targeting receptor binding domain of SARS-CoV-2 spike protein , 2021, Nature communications.
[54] D. Ho,et al. Potent SARS-CoV-2 neutralizing antibodies directed against spike N-terminal domain target a single supersite , 2021, bioRxiv.
[55] M. Nussenzweig,et al. SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies , 2020, Nature.
[56] A. Griffiths,et al. A trimeric human angiotensin-converting enzyme 2 as an anti-SARS-CoV-2 agent , 2020, Nature Structural & Molecular Biology.
[57] J. Dye,et al. Engineering human ACE2 to optimize binding to the spike protein of SARS coronavirus 2 , 2020, Science.
[58] J. Sodroski,et al. Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike , 2020, Nature.
[59] J. Sodroski,et al. Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike , 2020, Nature.
[60] Qiang Zhou,et al. A neutralizing human antibody binds to the N-terminal domain of the Spike protein of SARS-CoV-2 , 2020, Science.
[61] M. Kiso,et al. The Anticoagulant Nafamostat Potently Inhibits SARS-CoV-2 S Protein-Mediated Fusion in a Cell Fusion Assay System and Viral Infection In Vitro in a Cell-Type-Dependent Manner , 2020, Viruses.
[62] Ilya J. Finkelstein,et al. Structure-based Design of Prefusion-stabilized SARS-CoV-2 Spikes , 2020, bioRxiv.
[63] Amalio Telenti,et al. Cross-neutralization of SARS-CoV-2 by a human monoclonal SARS-CoV antibody , 2020, Nature.
[64] S. Kishigami,et al. Super-rapid quantitation of the production of HIV-1 harboring a luminescent peptide tag , 2020, The Journal of Biological Chemistry.
[65] Linqi Zhang,et al. Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor , 2020, Nature.
[66] Fumihiro Kato,et al. Enhanced isolation of SARS-CoV-2 by TMPRSS2-expressing cells , 2020, Proceedings of the National Academy of Sciences.
[67] Jia Gu,et al. fastp: an ultra-fast all-in-one FASTQ preprocessor , 2018, bioRxiv.
[68] Conrad C. Huang,et al. UCSF ChimeraX: Meeting modern challenges in visualization and analysis , 2018, Protein science : a publication of the Protein Society.
[69] Yutaka Suzuki,et al. Long-term expansion of alveolar stem cells derived from human iPS cells in organoids , 2017, Nature Methods.
[70] Heng Li,et al. Minimap2: pairwise alignment for nucleotide sequences , 2017, Bioinform..
[71] Jiahui Chen,et al. Improvements to the APBS biomolecular solvation software suite , 2017, Protein science : a publication of the Protein Society.
[72] David J. Fleet,et al. cryoSPARC: algorithms for rapid unsupervised cryo-EM structure determination , 2017, Nature Methods.
[73] S. Muro,et al. Directed Induction of Functional Multi-ciliated Cells in Proximal Airway Epithelial Spheroids from Human Pluripotent Stem Cells , 2015, Stem cell reports.
[74] S. Ogawa,et al. Generation of Alveolar Epithelial Spheroids via Isolated Progenitor Cells from Human Pluripotent Stem Cells , 2014, Stem cell reports.
[75] Alexandros Stamatakis,et al. RAxML version 8: a tool for phylogenetic analysis and post-analysis of large phylogenies , 2014, Bioinform..
[76] A. Steven,et al. One number does not fit all: mapping local variations in resolution in cryo-EM reconstructions. , 2013, Journal of structural biology.
[77] Pablo Cingolani,et al. © 2012 Landes Bioscience. Do not distribute. , 2022 .
[78] N. Kondo,et al. Monitoring Viral‐Mediated Membrane Fusion Using Fluorescent Reporter Methods , 2011, Current protocols in cell biology.
[79] Y. Yanagi,et al. Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM , 2011, Nature Structural &Molecular Biology.
[80] Toni Gabaldón,et al. trimAl: a tool for automated alignment trimming in large-scale phylogenetic analyses , 2009, Bioinform..
[81] Gonçalo R. Abecasis,et al. The Sequence Alignment/Map format and SAMtools , 2009, Bioinform..
[82] Richard Durbin,et al. Sequence analysis Fast and accurate short read alignment with Burrows – Wheeler transform , 2009 .
[83] Kevin Cowtan,et al. research papers Acta Crystallographica Section D Biological , 2005 .
[84] Conrad C. Huang,et al. UCSF Chimera—A visualization system for exploratory research and analysis , 2004, J. Comput. Chem..
[85] H. Niwa,et al. Efficient selection for high-expression transfectants with a novel eukaryotic vector. , 1991, Gene.
[86] Eleanor,et al. Altered TMPRSS2 usage by SARS-CoV-2 Omicron impacts tropism and fusogenicity , 2022 .
[87] Nasser,et al. Virological characteristics of the novel SARS-CoV-2 Omicron variants 1 including BA . 2 , 2022 .
[88] Christopher J. Williams,et al. MolProbity: More and better reference data for improved all‐atom structure validation , 2018, Protein science : a publication of the Protein Society.
[89] Claude-Alain H. Roten,et al. Fast and accurate short read alignment with Burrows–Wheeler transform , 2009, Bioinform..