Sự thoát khỏi kháng thể trung hoà của các biến thể protein gai SARS-CoV-2
Tóm tắt
Kháng thể trung hoà được tạo ra bởi nhiễm trùng trước đó hoặc tiêm chủng có khả năng đóng vai trò quan trọng trong việc bảo vệ tương lai cho cá nhân và quần thể chống lại SARS-CoV-2. Hơn nữa, các kháng thể được tiêm chủng một cách thụ động nằm trong số những tác nhân điều trị và dự phòng chống SARS-CoV-2 khả thi nhất. Tuy nhiên, mức độ mà SARS-CoV-2 sẽ thích nghi để né tránh các kháng thể trung hoà vẫn chưa rõ ràng. Sử dụng virus báo cáo VSV/SARS-CoV-2 tái tổ hợp, chúng tôi cho thấy rằng các biến thể protein S của SARS-CoV-2 chức năng có đột biến trong miền liên kết thụ thể (RBD) và miền đầu N mà mang lại khả năng kháng lại các kháng thể đơn dòng hoặc huyết tương hồi phục có thể dễ dàng được chọn lọc. Đáng chú ý, các biến thể S của SARS-CoV-2 kháng lại các kháng thể trung hoà thường được tạo ra hiện đang xuất hiện với tần suất thấp trong các quần thể SARS-CoV-2 lưu hành. Cuối cùng, sự xuất hiện của các biến thể SARS-CoV-2 kháng kháng thể mà có thể hạn chế tính hữu ích điều trị của các kháng thể đơn dòng có thể được giảm thiểu bằng cách sử dụng các tổ hợp kháng thể nhằm vào các epitope trung hoà khác nhau.
Từ khóa
Tài liệu tham khảo
Al‐Riyami, 2020, Clinical use of convalescent plasma in the covid‐19 pandemic: a transfusion‐focussed gap analysis with recommendations for future research priorities, Vox Sanguinis, 158, 10.1111/vox.12973
Barnes, 2020, Structures of human antibodies bound to SARS-CoV-2 spike reveal common epitopes and recurrent features of antibodies, Cell, 182, 828, 10.1016/j.cell.2020.06.025
Baum, 2020, Antibody cocktail to SARS-CoV-2 spike protein prevents rapid mutational escape seen with individual antibodies, Science, 369, 0831, 10.1126/science.abd0831
Bloch, 2020, Deployment of convalescent plasma for the prevention and treatment of COVID-19, Journal of Clinical Investigation, 130, 2757, 10.1172/JCI138745
Brouwer, 2020, Potent neutralizing antibodies from COVID-19 patients define multiple targets of vulnerability, Science, 369, 643, 10.1126/science.abc5902
Cao, 2020, Potent Neutralizing Antibodies against SARS-CoV-2 Identified by High-Throughput Single-Cell Sequencing of Convalescent Patients’ B Cells, Cell, 182, 73, 10.1016/j.cell.2020.05.025
Chen, 2020, Human monoclonal antibodies block the binding of SARS-CoV-2 spike protein to angiotensin converting enzyme 2 receptor, Cellular & Molecular Immunology, 17, 647, 10.1038/s41423-020-0426-7
Chi, 2020, A potent neutralizing human antibody reveals the N-terminal domain of the spike protein of SARS-CoV-2 as a site of vulnerability, bioRxiv, 10.1101/2020.05.08.083964
Combe, 2014, Variation in RNA Virus Mutation Rates across Host Cells, PLOS Pathogens, 10, 10.1371/journal.ppat.1003855
Dearlove, 2020, A SARS-CoV-2 vaccine candidate would likely match all currently circulating variants, PNAS, 117, 23652, 10.1073/pnas.2008281117
Denison, 2011, Coronaviruses: an RNA proofreading machine regulates replication fidelity and diversity, RNA Biology, 8, 270, 10.4161/rna.8.2.15013
Dolan, 2018, Mapping the Evolutionary Potential of RNA Viruses, Cell Host & Microbe, 23, 435, 10.1016/j.chom.2018.03.012
Duffy, 2008, Rates of evolutionary change in viruses: patterns and determinants, Nature Reviews Genetics, 9, 267, 10.1038/nrg2323
Elbe, 2017, Data, disease and diplomacy: GISAID's innovative contribution to global health, Global Challenges, 1, 33, 10.1002/gch2.1018
Gaebler, 2019, Combination of quadruplex qPCR and next-generation sequencing for qualitative and quantitative analysis of the HIV-1 latent reservoir, Journal of Experimental Medicine, 216, 2253, 10.1084/jem.20190896
Greaney, 2020, Complete mapping of mutations to the SARS-CoV-2 spike receptor-binding domain that escape antibody recognition, bioRxiv, 10.1101/2020.09.10.292078
Hansen, 2020, Studies in humanized mice and convalescent humans yield a SARS-CoV-2 antibody cocktail, Science, 369, 1010, 10.1126/science.abd0827
Hsieh, 2020, Structure-based design of prefusion-stabilized SARS-CoV-2 spikes, Science, 369, 1501, 10.1126/science.abd0826
Ju, 2020, Human neutralizing antibodies elicited by SARS-CoV-2 infection, Nature, 584, 115, 10.1038/s41586-020-2380-z
Kellam, 2020, The dynamics of humoral immune responses following SARS-CoV-2 infection and the potential for reinfection, Journal of General Virology, 101, 791, 10.1099/jgv.0.001439
Kk, 2020, COVID-19 re-infection by a phylogenetically distinct SARS-coronavirus-2 strain confirmed by whole genome sequencing, Clinical Infectious Diseases, 25, 10.1093/cid/ciaa1275
Kk, 2020, Serum antibody profile of a patient with COVID-19 reinfection, Clinical Infectious Diseases, 23, 10.1093/cid/ciaa1368
Korber, 2020, Tracking changes in SARS-CoV-2 spike: evidence that D614G increases infectivity of the COVID-19 virus, Cell, 182, 812, 10.1016/j.cell.2020.06.043
Kreer, 2020, Longitudinal isolation of potent Near-Germline SARS-CoV-2-Neutralizing antibodies from COVID-19 patients, Cell, 182, 1663, 10.1016/j.cell.2020.08.046
Larson, 2020, A case of early Re-infection with SARS-CoV-2, Clinical Infectious Diseases, 19, 10.1093/cid/ciaa1436
Liu, 2020, Potent neutralizing antibodies against multiple epitopes on SARS-CoV-2 spike, Nature, 584, 450, 10.1038/s41586-020-2571-7
Luchsinger, 2020, Serological assays estimate highly variable SARS-CoV-2 neutralizing antibody activity in recovered COVID19 patients, Journal of Clinical Microbiology, 11, 10.1128/JCM.02005-20
Moya, 2000, The evolution of RNA viruses: A population genetics view, PNAS, 97, 6967, 10.1073/pnas.97.13.6967
Plotkin, 2010, Correlates of protection induced by vaccination, Clinical and Vaccine Immunology, 17, 1055, 10.1128/CVI.00131-10
Rambaut, 2020, A dynamic nomenclature proposal for SARS-CoV-2 lineages to assist genomic epidemiology, Nature Microbiology, 5, 1403, 10.1038/s41564-020-0770-5
Rausch, 2020, Low genetic diversity may be an achilles heel of SARS-CoV-2, PNAS, 117, 24614, 10.1073/pnas.2017726117
Robbiani, 2020, Convergent antibody responses to SARS-CoV-2 in convalescent individuals, Nature, 584, 437, 10.1038/s41586-020-2456-9
Rogers, 2020, Isolation of potent SARS-CoV-2 neutralizing antibodies and protection from disease in a small animal model, Science, 369, eabc7520, 10.1126/science.abc7520
Schmidt, 2020, Measuring SARS-CoV-2 neutralizing antibody activity using pseudotyped and chimeric viruses, Journal of Experimental Medicine, 217, 10.1084/jem.20201181
Seydoux, 2020, Analysis of a SARS-CoV-2-Infected individual reveals development of potent neutralizing antibodies with limited somatic mutation, Immunity, 53, 98, 10.1016/j.immuni.2020.06.001
Shi, 2020, A human neutralizing antibody targets the receptor-binding site of SARS-CoV-2, Nature, 584, 120, 10.1038/s41586-020-2381-y
Singer, 2020, CoV-GLUE: a web application for tracking SARS-CoV-2 genomic variation, Preprints, 10.20944/preprints202006.0225.v1
Steinhauer, 1989, High nucleotide substitution error frequencies in clonal pools of vesicular stomatitis virus, Journal of Virology, 63, 2063, 10.1128/JVI.63.5.2063-2071.1989
Steinhauer, 1986, Direct method for quantitation of extreme polymerase error frequencies at selected single base sites in viral RNA, Journal of Virology, 57, 219, 10.1128/JVI.57.1.219-228.1986
van Dorp, 2020, Emergence of genomic diversity and recurrent mutations in SARS-CoV-2, Infection, Genetics and Evolution, 83, 10.1016/j.meegid.2020.104351
Van Elslande, 2020, Symptomatic SARS-CoV-2 reinfection by a phylogenetically distinct strain, Clinical Infectious Diseases, 5, 10.1093/cid/ciaa1330
Wang, 2020, Enhanced SARS-CoV-2 neutralization by secretory IgA in vitro, bioRxiv, 10.1101/2020.09.09.288555
Wec, 2020, Broad neutralization of SARS-related viruses by human monoclonal antibodies, Science, 369, 731, 10.1126/science.abc7424
Wölfel, 2020, Virological assessment of hospitalized patients with COVID-2019, Nature, 581, 465, 10.1038/s41586-020-2196-x
Wu Y, Wang F, Shen C, Peng W, Li D, Zhao C. 2020a. A non-competing pair of human neutralizing antibodies block COVID-19 virus binding to its receptor ACE2. medRxiv. https://science.sciencemag.org/content/368/6496/1274.
Wu F, Wang A, Liu M, Wang Q, Chen J, Xia S. 2020b. Neutralizing antibody responses to SARS-CoV-2 in a COVID-19 recovered patient cohort and their implications. medRxiv. https://www.medrxiv.org/content/10.1101/2020.03.30.20047365v2.
Yan, 2020, Structural basis for the recognition of SARS-CoV-2 by full-length human ACE2, Science, 367, 1444, 10.1126/science.abb2762
Yuan, 2020, Structural basis of a shared antibody response to SARS-CoV-2, Science, 369, 1119, 10.1126/science.abd2321