Kháng thể người có nguồn gốc từ nhiễm SARS-CoV-2 ban đầu trung hòa hiệu quả biến thể Omicron
Tóm tắt
Từ khóa
Tài liệu tham khảo
Barnes CO, et al. SARS-CoV-2 neutralizing antibody structures inform therapeutic strategies. Nature. 2020;588:682–7.
Barnes CO, et al. Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies. Cell. 2020;182:828–42 e16.
Brouwer PJM, et al. Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability. Science. 2020;369:643–50.
Cameroni E, et al. Broadly neutralizing antibodies overcome SARS-CoV-2 Omicron antigenic shift. Nature. 2022;602:664–70.
Cao Y, et al. Potent Neutralizing Antibodies against SARS-CoV-2 Identified by High-Throughput Single-Cell Sequencing of Convalescent Patients’ B Cells. Cell. 2020;182:73–84 e16.
Cao Y, et al. Omicron escapes the majority of existing SARS-CoV-2 neutralizing antibodies. Nature. 2022;602:657–63.
Chen RE, et al. Resistance of SARS-CoV-2 variants to neutralization by monoclonal and serum-derived polyclonal antibodies. Nat Med. 2021;27:717–26.
Cui Z, et al. Structural and functional characterizations of infectivity and immune evasion of SARS-CoV-2 Omicron. Cell. 2022;185:860–71 e13.
Dejnirattisai W, et al. The antigenic anatomy of SARS-CoV-2 receptor binding domain. Cell. 2021;184:2183–200 e22.
Greaney AJ, et al. Complete Mapping of Mutations to the SARS-CoV-2 Spike Receptor-Binding Domain that Escape Antibody Recognition. Cell Host Microbe. 2021;29:44–57 e9.
Hansen J, et al. Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail. Science. 2020;369:1010–4.
Hastie KM, et al. Defining variant-resistant epitopes targeted by SARS-CoV-2 antibodies: A global consortium study. Science. 2021;374:472–8.
Henderson R, et al. Controlling the SARS-CoV-2 spike glycoprotein conformation. Nat Struct Mol Biol. 2020;27:925–33.
Hoffmann M, et al. SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor. Cell. 2020;181:271–280.e8.
Huo J, et al. Neutralization of SARS-CoV-2 by Destruction of the Prefusion Spike. Cell Host Microbe. 2020;28:445–54 e6.
Iketani S, et al. Antibody evasion properties of SARS-CoV-2 Omicron sublineages. Nature. 2022;604:553–6.
Lan J, et al. Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor. Nature. 2020;581:215–20.
Li T, et al. Uncovering a conserved vulnerability site in SARS-CoV-2 by a human antibody. EMBO Mol Med. 2021a;13: e14544.
Li T, et al. A synthetic nanobody targeting RBD protects hamsters from SARS-CoV-2 infection. Nat Commun. 2021b;12:4635.
Li T, et al. A synthetic nanobody targeting RBD protects hamsters from SARS-CoV-2 infection. Nat Commun. 2021c;12:4635.
Li T, et al. Isolation, characterization, and structure-based engineering of a neutralizing nanobody against SARS-CoV-2. Int J Biol Macromol. 2022a;209:1379–88.
Li T, et al. Structural Characterization of a Neutralizing Nanobody With Broad Activity Against SARS-CoV-2 Variants. Front Microbiol. 2022b;13: 875840.
Liu H, et al. Cross-Neutralization of a SARS-CoV-2 Antibody to a Functionally Conserved Site Is Mediated by Avidity. Immunity. 2020;53:1272–80 e5.
Liu L, et al. Striking antibody evasion manifested by the Omicron variant of SARS-CoV-2. Nature. 2022;602:676–81.
Liu, Z. et al. An ultrapotent pan-beta-coronavirus lineage B (beta-CoV-B) neutralizing antibody locks the receptor-binding domain in closed conformation by targeting its conserved epitope. Protein Cell (2021).
Lv Z, et al. Structural basis for neutralization of SARS-CoV-2 and SARS-CoV by a potent therapeutic antibody. Science. 2020;369:1505–9.
McCallum M, et al. Structural basis of SARS-CoV-2 Omicron immune evasion and receptor engagement. Science. 2022;375:864–8.
Meng L, et al. A Spike-destructing human antibody effectively neutralizes Omicron-included SARS-CoV-2 variants with therapeutic efficacy. PLoS Pathog. 2023;19: e1011085.
Nabel, K.G. et al. Structural basis for continued antibody evasion by the SARS-CoV-2 receptor binding domain. Science 375, eabl6251 (2022).
Piccoli L, et al. Mapping Neutralizing and Immunodominant Sites on the SARS-CoV-2 Spike Receptor-Binding Domain by Structure-Guided High-Resolution Serology. Cell. 2020;183:1024–42 e21.
Planas D, et al. Considerable escape of SARS-CoV-2 Omicron to antibody neutralization. Nature. 2022;602:671–5.
Schoof M, et al. An ultrapotent synthetic nanobody neutralizes SARS-CoV-2 by stabilizing inactive Spike. Science. 2020;370:1473–9.
Sheward, D.J. et al. Neutralisation sensitivity of the SARS-CoV-2 omicron (B.1.1.529) variant: a cross-sectional study. Lancet Infect Dis (2022).
Shi R, et al. A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2. Nature. 2020;584:120–4.
Starr TN, et al. Deep Mutational Scanning of SARS-CoV-2 Receptor Binding Domain Reveals Constraints on Folding and ACE2 Binding. Cell. 2020;182:1295–310 e20.
Starr TN, et al. SARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape. Nature. 2021;597:97–102.
Tuekprakhon A, et al. Antibody escape of SARS-CoV-2 Omicron BA.4 and BA.5 from vaccine and BA.1 serum. Cell. 2022;185:2422–2433. e13.
VanBlargan LA, et al. An infectious SARS-CoV-2 B.1.1.529Omicron virus escapes neutralization by therapeutic monoclonal antibodies. Nat Med. 2022;28:490–5.
Walls AC, et al. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Cell. 2020;181:281–292.e6.
Watanabe Y, Allen JD, Wrapp D, McLellan JS, Crispin M. Site-specific glycan analysis of the SARS-CoV-2 spike. Science. 2020;369:330–3.
Wrapp D, et al. Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation. Science. 2020;367:1260–3.
Yamin R, et al. Fc-engineered antibody therapeutics with improved anti-SARS-CoV-2 efficacy. Nature. 2021;599:465–70.
Yao H, et al. A high-affinity RBD-targeting nanobody improves fusion partner’s potency against SARS-CoV-2. PLoS Pathog. 2021;17:e1009328.