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DOI10.1073/pnas.2103154118
SARS-CoV-2 escape from a highly neutralizing COVID-19 convalescent plasma
Andreano E.; Piccini G.; Licastro D.; Casalino L.; Johnson N.V.; Paciello I.; Monego S.D.; Pantano E.; Manganaro N.; Manenti A.; Manna R.; Casa E.; Hyseni I.; Benincasa L.; Montomoli E.; Amaro R.E.; McLellan J.S.; Rappuoli R.
发表日期2021
ISSN0027-8424
卷号118期号:36
英文摘要To investigate the evolution of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) in the immune population, we coin-cupi bated the authentic virus with a highly neutralizing plasma from a COVID-19 convalescent patient. The plasma fully neutralized the virus for seven passages, but, after 45 d, the deletion of F140 in the spike N-terminal domain (NTD) N3 loop led to partial breakthrough. At day 73, an E484K substitution in the receptor-binding domain (RBD) occurred, followed, at day 80, by an insertion in the NTD N5 loop containing a new glycan sequon, which generated a variant completely resistant to plasma neutralization. Computational modeling predicts that the deletion and insertion in loops N3 and N5 prevent binding of neutralizing antibodies. The recent emergence in the United Kingdom, South Africa, Brazil, and Japan of natural variants with similar changes suggests that SARS-CoV-2 has the potential to escape an effective immune response and that vaccines and antibodies able to control emerging variants should be developed. © 2021 National Academy of Sciences. All rights reserved.
英文关键词Antibody response; COVID-19; Emerging variants; Immune evasion; SARS-CoV-2
语种英语
scopus关键词neutralizing antibody; SARS-CoV-2 convalescent plasma; vitronectin; ACE2 protein, human; antiserum; coronavirus spike glycoprotein; neutralizing antibody; protein binding; spike protein, SARS-CoV-2; virus antibody; amino terminal sequence; antigen binding; Article; clinical article; computer model; controlled study; gene mutation; genetic variability; human; immune response; nonhuman; protein domain; receptor binding; Severe acute respiratory syndrome coronavirus 2; virus load; virus neutralization; alpha helix; amino acid substitution; animal; beta sheet; binding site; chemistry; Chlorocebus aethiops; convalescence; drug effect; gene expression; genetics; immune evasion; immunology; molecular model; mutation; pathogenicity; serodiagnosis; Vero cell line; virology; Amino Acid Substitution; Angiotensin-Converting Enzyme 2; Animals; Antibodies, Neutralizing; Antibodies, Viral; Binding Sites; Chlorocebus aethiops; Convalescence; COVID-19; Gene Expression; Humans; Immune Evasion; Immune Sera; Models, Molecular; Mutation; Neutralization Tests; Protein Binding; Protein Conformation, alpha-Helical; Protein Conformation, beta-Strand; Protein Interaction Domains and Motifs; SARS-CoV-2; Spike Glycoprotein, Coronavirus; Vero Cells
来源期刊Proceedings of the National Academy of Sciences of the United States of America
文献类型期刊论文
条目标识符http://gcip.llas.ac.cn/handle/2XKMVOVA/238812
作者单位Monoclonal Antibody Discovery Lab, Fondazione Toscana Life Sciences, Siena, 53100, Italy; VisMederi S.r.l., Siena, 53100, Italy; ARGO Open Lab Platform for Genome Sequencing, Trieste, 34149, Italy; Department of Chemistry and Biochemistry, University of California San Diego, San diego, CA 92093, United States; Department of Molecular Biosciences, University of Texas at Austin, Austin, TX 78712, United States; VisMederi Research S.r.l., Siena, 53100, Italy; Department of Molecular and Developmental Medicine, University of Siena, Siena, 53100, Italy; Faculty of Medicine, Imperial College, London, SW7 2DD, United Kingdom
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GB/T 7714
Andreano E.,Piccini G.,Licastro D.,et al. SARS-CoV-2 escape from a highly neutralizing COVID-19 convalescent plasma[J],2021,118(36).
APA Andreano E..,Piccini G..,Licastro D..,Casalino L..,Johnson N.V..,...&Rappuoli R..(2021).SARS-CoV-2 escape from a highly neutralizing COVID-19 convalescent plasma.Proceedings of the National Academy of Sciences of the United States of America,118(36).
MLA Andreano E.,et al."SARS-CoV-2 escape from a highly neutralizing COVID-19 convalescent plasma".Proceedings of the National Academy of Sciences of the United States of America 118.36(2021).
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