In vitro data suggest that Indian delta variant B.1.617 of SARS‐CoV‐2 escapes neutralization by both receptor affinity and immune evasion
Background Emerged mutations can be attributed to increased transmissibility of the B.1.617 and B.1.36 Indian delta variants of SARS‐CoV‐2, most notably substitutions L452R/E484Q and N440K, respectively, which occur in the receptor‐binding domain (RBD) of the Spike (S) fusion glycoprotein. Objective...
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| Published in | Allergy (Copenhagen) Vol. 77; no. 1; pp. 111 - 117 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Denmark
Blackwell Publishing Ltd
01.01.2022
John Wiley and Sons Inc |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0105-4538 1398-9995 1398-9995 |
| DOI | 10.1111/all.15065 |
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| Abstract | Background
Emerged mutations can be attributed to increased transmissibility of the B.1.617 and B.1.36 Indian delta variants of SARS‐CoV‐2, most notably substitutions L452R/E484Q and N440K, respectively, which occur in the receptor‐binding domain (RBD) of the Spike (S) fusion glycoprotein.
Objective
We aimed to assess the effects of mutations L452R/E484Q and N440K (as well as the previously studied mutation E484K present in variants B.1.351 and P.1) on the affinity of RBD for ACE2, SARS‐CoV‐2 main receptor. We also aimed to assess the ability of antibodies induced by natural infection or by immunization with BNT162b2 mRNA vaccine to recognize the mutated versions of the RBD, as well as blocking the interaction RBD‐ACE2, an important surrogate readout for virus neutralization.
Methods
To this end, we produced recombinant wild‐type RBD, as well as RBD containing each of the mutations L452R/E484Q, N440K, or E484K (the latest present in variants of concern B.1.351 and P.1), as well as the ectodomain of ACE2. Using Biolayer Interferometry (BLI), we measured the binding affinity of RBD for ACE2 and the ability of sera from COVID‐19 convalescent donors or subjects immunized with BNT162b2 mRNA vaccine to block this interaction. Finally, we correlated these results with total anti‐RBD IgG titers measured from the same sera by direct ELISA.
Results
The binding assays showed L452R/E484Q double‐mutant RBD to interact with ACE2 with higher affinity (KD = 4.6 nM) than wild‐type (KD = 21.3 nM) or single mutants N440K (KD = 9.9 nM) and E484K (KD = 19.7 nM) RBDs. Meanwhile, the anti‐RBD IgG titration resulted in lower recognition of mutants E484K and L452R/E484Q by infection‐induced antibodies, whereas only mutant E484K was recognized less by antibodies induced by vaccination. More interestingly, sera from convalescent as well as immunized subjects showed reduced ability to block the interaction between ACE2 and RBD mutants E484K and L452R/E484Q, as shown by the inhibition assays.
Conclusion
Our data suggest that the newly emerged SARS‐CoV‐2 variant B.1.617, as well as the better‐studied variants B.1.351 and P.1 (all containing a mutation at position E484) display increased transmissibility both due to their higher affinity for the cell receptor ACE2 and their ability to partially bypass immunity generated against the wild‐type virus. For variant B.1.36 (with a point mutation at position N440), only increased affinity seems to play a role.
Binding assays using Biolayer Interferometry showed that the RBD containing L452R/E484Q present in the new SARS‐CoV‐2 variant B.1.617 interacts with ACE2 with higher affinity than wild‐type or single mutants N440K and E484K. Sera from convalescent and BTN162b2 vaccinated individual showed reduced ability to block the interaction between ACE2 and RBD mutants E484K and L452R/E484Q suggesting that the new SARS‐CoV‐2 variant B.1.617 bypass immunity generated against the wild‐type virus. Abbreviations: ACE2, angiotensin‐converting enzyme 2; COVID‐19, coronavirus disease 2019; RBD, receptor binding domain; RBDE484K, RBD containing mutation E484K on S; RBDL452R/E484Q, RBD containing both mutations L452K and E484Q on S; RBDN440K, RBD containing mutation N440K on S; RBDWT, wild‐type RBD; SARS‐CoV‐2, severe acute respiratory syndrome coronavirus type 2 |
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| AbstractList | Emerged mutations can be attributed to increased transmissibility of the B.1.617 and B.1.36 Indian delta variants of SARS-CoV-2, most notably substitutions L452R/E484Q and N440K, respectively, which occur in the receptor-binding domain (RBD) of the Spike (S) fusion glycoprotein.BACKGROUNDEmerged mutations can be attributed to increased transmissibility of the B.1.617 and B.1.36 Indian delta variants of SARS-CoV-2, most notably substitutions L452R/E484Q and N440K, respectively, which occur in the receptor-binding domain (RBD) of the Spike (S) fusion glycoprotein.We aimed to assess the effects of mutations L452R/E484Q and N440K (as well as the previously studied mutation E484K present in variants B.1.351 and P.1) on the affinity of RBD for ACE2, SARS-CoV-2 main receptor. We also aimed to assess the ability of antibodies induced by natural infection or by immunization with BNT162b2 mRNA vaccine to recognize the mutated versions of the RBD, as well as blocking the interaction RBD-ACE2, an important surrogate readout for virus neutralization.OBJECTIVEWe aimed to assess the effects of mutations L452R/E484Q and N440K (as well as the previously studied mutation E484K present in variants B.1.351 and P.1) on the affinity of RBD for ACE2, SARS-CoV-2 main receptor. We also aimed to assess the ability of antibodies induced by natural infection or by immunization with BNT162b2 mRNA vaccine to recognize the mutated versions of the RBD, as well as blocking the interaction RBD-ACE2, an important surrogate readout for virus neutralization.To this end, we produced recombinant wild-type RBD, as well as RBD containing each of the mutations L452R/E484Q, N440K, or E484K (the latest present in variants of concern B.1.351 and P.1), as well as the ectodomain of ACE2. Using Biolayer Interferometry (BLI), we measured the binding affinity of RBD for ACE2 and the ability of sera from COVID-19 convalescent donors or subjects immunized with BNT162b2 mRNA vaccine to block this interaction. Finally, we correlated these results with total anti-RBD IgG titers measured from the same sera by direct ELISA.METHODSTo this end, we produced recombinant wild-type RBD, as well as RBD containing each of the mutations L452R/E484Q, N440K, or E484K (the latest present in variants of concern B.1.351 and P.1), as well as the ectodomain of ACE2. Using Biolayer Interferometry (BLI), we measured the binding affinity of RBD for ACE2 and the ability of sera from COVID-19 convalescent donors or subjects immunized with BNT162b2 mRNA vaccine to block this interaction. Finally, we correlated these results with total anti-RBD IgG titers measured from the same sera by direct ELISA.The binding assays showed L452R/E484Q double-mutant RBD to interact with ACE2 with higher affinity (KD = 4.6 nM) than wild-type (KD = 21.3 nM) or single mutants N440K (KD = 9.9 nM) and E484K (KD = 19.7 nM) RBDs. Meanwhile, the anti-RBD IgG titration resulted in lower recognition of mutants E484K and L452R/E484Q by infection-induced antibodies, whereas only mutant E484K was recognized less by antibodies induced by vaccination. More interestingly, sera from convalescent as well as immunized subjects showed reduced ability to block the interaction between ACE2 and RBD mutants E484K and L452R/E484Q, as shown by the inhibition assays.RESULTSThe binding assays showed L452R/E484Q double-mutant RBD to interact with ACE2 with higher affinity (KD = 4.6 nM) than wild-type (KD = 21.3 nM) or single mutants N440K (KD = 9.9 nM) and E484K (KD = 19.7 nM) RBDs. Meanwhile, the anti-RBD IgG titration resulted in lower recognition of mutants E484K and L452R/E484Q by infection-induced antibodies, whereas only mutant E484K was recognized less by antibodies induced by vaccination. More interestingly, sera from convalescent as well as immunized subjects showed reduced ability to block the interaction between ACE2 and RBD mutants E484K and L452R/E484Q, as shown by the inhibition assays.Our data suggest that the newly emerged SARS-CoV-2 variant B.1.617, as well as the better-studied variants B.1.351 and P.1 (all containing a mutation at position E484) display increased transmissibility both due to their higher affinity for the cell receptor ACE2 and their ability to partially bypass immunity generated against the wild-type virus. For variant B.1.36 (with a point mutation at position N440), only increased affinity seems to play a role.CONCLUSIONOur data suggest that the newly emerged SARS-CoV-2 variant B.1.617, as well as the better-studied variants B.1.351 and P.1 (all containing a mutation at position E484) display increased transmissibility both due to their higher affinity for the cell receptor ACE2 and their ability to partially bypass immunity generated against the wild-type virus. For variant B.1.36 (with a point mutation at position N440), only increased affinity seems to play a role. Background Emerged mutations can be attributed to increased transmissibility of the B.1.617 and B.1.36 Indian delta variants of SARS‐CoV‐2, most notably substitutions L452R/E484Q and N440K, respectively, which occur in the receptor‐binding domain (RBD) of the Spike (S) fusion glycoprotein. Objective We aimed to assess the effects of mutations L452R/E484Q and N440K (as well as the previously studied mutation E484K present in variants B.1.351 and P.1) on the affinity of RBD for ACE2, SARS‐CoV‐2 main receptor. We also aimed to assess the ability of antibodies induced by natural infection or by immunization with BNT162b2 mRNA vaccine to recognize the mutated versions of the RBD, as well as blocking the interaction RBD‐ACE2, an important surrogate readout for virus neutralization. Methods To this end, we produced recombinant wild‐type RBD, as well as RBD containing each of the mutations L452R/E484Q, N440K, or E484K (the latest present in variants of concern B.1.351 and P.1), as well as the ectodomain of ACE2. Using Biolayer Interferometry (BLI), we measured the binding affinity of RBD for ACE2 and the ability of sera from COVID‐19 convalescent donors or subjects immunized with BNT162b2 mRNA vaccine to block this interaction. Finally, we correlated these results with total anti‐RBD IgG titers measured from the same sera by direct ELISA. Results The binding assays showed L452R/E484Q double‐mutant RBD to interact with ACE2 with higher affinity (KD = 4.6 nM) than wild‐type (KD = 21.3 nM) or single mutants N440K (KD = 9.9 nM) and E484K (KD = 19.7 nM) RBDs. Meanwhile, the anti‐RBD IgG titration resulted in lower recognition of mutants E484K and L452R/E484Q by infection‐induced antibodies, whereas only mutant E484K was recognized less by antibodies induced by vaccination. More interestingly, sera from convalescent as well as immunized subjects showed reduced ability to block the interaction between ACE2 and RBD mutants E484K and L452R/E484Q, as shown by the inhibition assays. Conclusion Our data suggest that the newly emerged SARS‐CoV‐2 variant B.1.617, as well as the better‐studied variants B.1.351 and P.1 (all containing a mutation at position E484) display increased transmissibility both due to their higher affinity for the cell receptor ACE2 and their ability to partially bypass immunity generated against the wild‐type virus. For variant B.1.36 (with a point mutation at position N440), only increased affinity seems to play a role. Binding assays using Biolayer Interferometry showed that the RBD containing L452R/E484Q present in the new SARS‐CoV‐2 variant B.1.617 interacts with ACE2 with higher affinity than wild‐type or single mutants N440K and E484K. Sera from convalescent and BTN162b2 vaccinated individual showed reduced ability to block the interaction between ACE2 and RBD mutants E484K and L452R/E484Q suggesting that the new SARS‐CoV‐2 variant B.1.617 bypass immunity generated against the wild‐type virus. Abbreviations: ACE2, angiotensin‐converting enzyme 2; COVID‐19, coronavirus disease 2019; RBD, receptor binding domain; RBDE484K, RBD containing mutation E484K on S; RBDL452R/E484Q, RBD containing both mutations L452K and E484Q on S; RBDN440K, RBD containing mutation N440K on S; RBDWT, wild‐type RBD; SARS‐CoV‐2, severe acute respiratory syndrome coronavirus type 2 Binding assays using Biolayer Interferometry showed that the RBD containing L452R/E484Q present in the new SARS‐CoV‐2 variant B.1.617 interacts with ACE2 with higher affinity than wild‐type or single mutants N440K and E484K. Sera from convalescent and BTN162b2 vaccinated individual showed reduced ability to block the interaction between ACE2 and RBD mutants E484K and L452R/E484Q suggesting that the new SARS‐CoV‐2 variant B.1.617 bypass immunity generated against the wild‐type virus. Abbreviations: ACE2, angiotensin‐converting enzyme 2; COVID‐19, coronavirus disease 2019; RBD, receptor binding domain; RBDE484K, RBD containing mutation E484K on S; RBDL452R/E484Q, RBD containing both mutations L452K and E484Q on S; RBDN440K, RBD containing mutation N440K on S; RBDWT, wild‐type RBD; SARS‐CoV‐2, severe acute respiratory syndrome coronavirus type 2 Emerged mutations can be attributed to increased transmissibility of the B.1.617 and B.1.36 Indian delta variants of SARS-CoV-2, most notably substitutions L452R/E484Q and N440K, respectively, which occur in the receptor-binding domain (RBD) of the Spike (S) fusion glycoprotein. We aimed to assess the effects of mutations L452R/E484Q and N440K (as well as the previously studied mutation E484K present in variants B.1.351 and P.1) on the affinity of RBD for ACE2, SARS-CoV-2 main receptor. We also aimed to assess the ability of antibodies induced by natural infection or by immunization with BNT162b2 mRNA vaccine to recognize the mutated versions of the RBD, as well as blocking the interaction RBD-ACE2, an important surrogate readout for virus neutralization. To this end, we produced recombinant wild-type RBD, as well as RBD containing each of the mutations L452R/E484Q, N440K, or E484K (the latest present in variants of concern B.1.351 and P.1), as well as the ectodomain of ACE2. Using Biolayer Interferometry (BLI), we measured the binding affinity of RBD for ACE2 and the ability of sera from COVID-19 convalescent donors or subjects immunized with BNT162b2 mRNA vaccine to block this interaction. Finally, we correlated these results with total anti-RBD IgG titers measured from the same sera by direct ELISA. The binding assays showed L452R/E484Q double-mutant RBD to interact with ACE2 with higher affinity (K = 4.6 nM) than wild-type (K = 21.3 nM) or single mutants N440K (K = 9.9 nM) and E484K (K = 19.7 nM) RBDs. Meanwhile, the anti-RBD IgG titration resulted in lower recognition of mutants E484K and L452R/E484Q by infection-induced antibodies, whereas only mutant E484K was recognized less by antibodies induced by vaccination. More interestingly, sera from convalescent as well as immunized subjects showed reduced ability to block the interaction between ACE2 and RBD mutants E484K and L452R/E484Q, as shown by the inhibition assays. Our data suggest that the newly emerged SARS-CoV-2 variant B.1.617, as well as the better-studied variants B.1.351 and P.1 (all containing a mutation at position E484) display increased transmissibility both due to their higher affinity for the cell receptor ACE2 and their ability to partially bypass immunity generated against the wild-type virus. For variant B.1.36 (with a point mutation at position N440), only increased affinity seems to play a role. BackgroundEmerged mutations can be attributed to increased transmissibility of the B.1.617 and B.1.36 Indian delta variants of SARS‐CoV‐2, most notably substitutions L452R/E484Q and N440K, respectively, which occur in the receptor‐binding domain (RBD) of the Spike (S) fusion glycoprotein.ObjectiveWe aimed to assess the effects of mutations L452R/E484Q and N440K (as well as the previously studied mutation E484K present in variants B.1.351 and P.1) on the affinity of RBD for ACE2, SARS‐CoV‐2 main receptor. We also aimed to assess the ability of antibodies induced by natural infection or by immunization with BNT162b2 mRNA vaccine to recognize the mutated versions of the RBD, as well as blocking the interaction RBD‐ACE2, an important surrogate readout for virus neutralization.MethodsTo this end, we produced recombinant wild‐type RBD, as well as RBD containing each of the mutations L452R/E484Q, N440K, or E484K (the latest present in variants of concern B.1.351 and P.1), as well as the ectodomain of ACE2. Using Biolayer Interferometry (BLI), we measured the binding affinity of RBD for ACE2 and the ability of sera from COVID‐19 convalescent donors or subjects immunized with BNT162b2 mRNA vaccine to block this interaction. Finally, we correlated these results with total anti‐RBD IgG titers measured from the same sera by direct ELISA.ResultsThe binding assays showed L452R/E484Q double‐mutant RBD to interact with ACE2 with higher affinity (KD = 4.6 nM) than wild‐type (KD = 21.3 nM) or single mutants N440K (KD = 9.9 nM) and E484K (KD = 19.7 nM) RBDs. Meanwhile, the anti‐RBD IgG titration resulted in lower recognition of mutants E484K and L452R/E484Q by infection‐induced antibodies, whereas only mutant E484K was recognized less by antibodies induced by vaccination. More interestingly, sera from convalescent as well as immunized subjects showed reduced ability to block the interaction between ACE2 and RBD mutants E484K and L452R/E484Q, as shown by the inhibition assays.ConclusionOur data suggest that the newly emerged SARS‐CoV‐2 variant B.1.617, as well as the better‐studied variants B.1.351 and P.1 (all containing a mutation at position E484) display increased transmissibility both due to their higher affinity for the cell receptor ACE2 and their ability to partially bypass immunity generated against the wild‐type virus. For variant B.1.36 (with a point mutation at position N440), only increased affinity seems to play a role. |
| Author | Augusto, Gilles Vogel, Monique Bachmann, Martin F. Liu, Xuelan Zinkhan, Simon Mohsen, Mona O. |
| AuthorAffiliation | 1 Department of Immunology University clinic of Rheumatology and Immunology, Inselspital Bern Switzerland 4 International Immunology Centre Anhui Agricultural University Hefei China 2 Department of BioMedical Research University of Bern Bern Switzerland 3 The Jenner Institute University of Oxford Oxford UK |
| AuthorAffiliation_xml | – name: 2 Department of BioMedical Research University of Bern Bern Switzerland – name: 3 The Jenner Institute University of Oxford Oxford UK – name: 4 International Immunology Centre Anhui Agricultural University Hefei China – name: 1 Department of Immunology University clinic of Rheumatology and Immunology, Inselspital Bern Switzerland |
| Author_xml | – sequence: 1 givenname: Gilles orcidid: 0000-0001-6509-0148 surname: Augusto fullname: Augusto, Gilles organization: University of Oxford – sequence: 2 givenname: Mona O. surname: Mohsen fullname: Mohsen, Mona O. organization: University of Bern – sequence: 3 givenname: Simon orcidid: 0000-0001-6023-6224 surname: Zinkhan fullname: Zinkhan, Simon organization: University of Bern – sequence: 4 givenname: Xuelan surname: Liu fullname: Liu, Xuelan organization: Anhui Agricultural University – sequence: 5 givenname: Monique orcidid: 0000-0002-5219-4033 surname: Vogel fullname: Vogel, Monique organization: University of Bern – sequence: 6 givenname: Martin F. surname: Bachmann fullname: Bachmann, Martin F. email: martin.bachmann@dbmr.unibe.ch organization: Anhui Agricultural University |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/34453338$$D View this record in MEDLINE/PubMed |
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| Keywords | SARS-CoV-2 vaccine RBD neutralization affinity |
| Language | English |
| License | Attribution-NonCommercial-NoDerivs 2021 The Authors. Allergy published by European Academy of Allergy and Clinical Immunology and John Wiley & Sons Ltd. This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
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| References | 2021; 9 2021; 27 2017; 7 2021; 76 2021 2021; 29 2020; 181 2020; 16 2021; 593 2020; 584 2021; 372 2021; 592 2022; 77 2021; 154 e_1_2_9_11_1 e_1_2_9_10_1 e_1_2_9_13_1 e_1_2_9_12_1 e_1_2_9_8_1 e_1_2_9_7_1 e_1_2_9_5_1 e_1_2_9_4_1 e_1_2_9_3_1 Wu L (e_1_2_9_19_1) 2021 e_1_2_9_2_1 e_1_2_9_9_1 e_1_2_9_15_1 Jangra S (e_1_2_9_6_1) 2021 e_1_2_9_14_1 e_1_2_9_17_1 e_1_2_9_16_1 e_1_2_9_18_1 |
| References_xml | – year: 2021 article-title: The E484K mutation in the SARS‐CoV‐2 spike protein reduces but does not abolish neutralizing activity of human convalescent and post‐vaccination sera publication-title: medRxiv – volume: 77 start-page: 143 year: 2022 end-page: 149 article-title: Molecular definition of SARS‐CoV‐2 RBD mutations: receptor affinity versus neutralization of receptor interaction publication-title: Allergy – volume: 76 start-page: 2895 year: 2021 end-page: 2998 article-title: BNT162b2 mRNA COVID‐19 vaccine induces antibodies of broader cross‐reactivity than natural infection, but recognition of mutant viruses is up to 10‐fold reduced publication-title: Allergy – volume: 181 start-page: 894 issue: 4 year: 2020 end-page: 904. e899 article-title: Structural and functional basis of SARS‐CoV‐2 entry by using human ACE2 publication-title: Cell – volume: 372 start-page: 815 issue: 6544 year: 2021 end-page: 821 article-title: Genomics and epidemiology of the P.1 SARS‐CoV‐2 lineage in Manaus, Brazil publication-title: Science – volume: 16 issue: 12 year: 2020 article-title: A natural mutation between SARS‐CoV‐2 and SARS‐CoV determines neutralization by a cross‐reactive antibody publication-title: PLoS Pathog – volume: 76 start-page: 853 issue: 3 year: 2021 end-page: 865 article-title: Accuracy of serological testing for SARS‐CoV‐2 antibodies: first results of a large mixed‐method evaluation study publication-title: Allergy – volume: 27 start-page: 620 issue: 4 year: 2021 end-page: 621 article-title: Neutralization of SARS‐CoV‐2 spike 69/70 deletion, E484K and N501Y variants by BNT162b2 vaccine‐elicited sera publication-title: Nat Med – volume: 593 start-page: 321 year: 2021 article-title: Coronavirus variants are spreading in India‐What scientists know so far publication-title: Nature – volume: 29 start-page: 516 issue: 4 year: 2021 end-page: 521. e513 article-title: Infection‐ and vaccine‐induced antibody binding and neutralization of the B.1.351 SARS‐CoV‐2 variant publication-title: Cell Host Microbe – volume: 584 start-page: 437 issue: 7821 year: 2020 end-page: 442 article-title: Convergent antibody responses to SARS‐CoV‐2 infection in convalescent individuals publication-title: Nature – year: 2021 article-title: SARS‐CoV‐2 B.1.617 mutations L452 and E484Q are not synergistic for antibody evasion publication-title: J Infect Dis – volume: 7 start-page: 49 issue: 4 year: 2017 article-title: Strategies using bio‐layer interferometry biosensor technology for vaccine research and development publication-title: Biosensors (Basel) – volume: 154 start-page: 104831 year: 2021 article-title: Mutations in SARS‐CoV‐2; consequences in structure, function, and pathogenicity of the virus publication-title: Microb Pathog – volume: 592 start-page: 438 issue: 7854 year: 2021 end-page: 443 article-title: Detection of a SARS‐CoV‐2 variant of concern in South Africa publication-title: Nature – volume: 9 start-page: 243 issue: 3 year: 2021 article-title: Emerging SARS‐CoV‐2 variants and impact in global vaccination programs against SARS‐CoV‐2/COVID‐19 publication-title: Vaccines (Basel) – year: 2021 article-title: Predicting the potential effect of E484K mutation on the binding of 28 antibodies to the spike protein of SARS‐CoV‐2 by molecular dynamics simulation and free energy calculation publication-title: ChemRxiv – ident: e_1_2_9_8_1 doi: 10.1038/s41591-021-01270-4 – ident: e_1_2_9_2_1 doi: 10.1038/s41586-020-2456-9 – ident: e_1_2_9_13_1 doi: 10.1111/all.15002 – ident: e_1_2_9_3_1 doi: 10.1371/journal.ppat.1009089 – ident: e_1_2_9_9_1 doi: 10.1126/science.abh2644 – ident: e_1_2_9_17_1 doi: 10.1016/j.chom.2021.03.009 – ident: e_1_2_9_12_1 doi: 10.3390/bios7040049 – ident: e_1_2_9_7_1 doi: 10.3390/vaccines9030243 – year: 2021 ident: e_1_2_9_6_1 article-title: The E484K mutation in the SARS‐CoV‐2 spike protein reduces but does not abolish neutralizing activity of human convalescent and post‐vaccination sera publication-title: medRxiv – ident: e_1_2_9_10_1 doi: 10.1038/s41586-021-03402-9 – ident: e_1_2_9_14_1 doi: 10.1111/all.14893 – ident: e_1_2_9_18_1 doi: 10.1093/infdis/jiab368 – ident: e_1_2_9_4_1 doi: 10.1111/all.14608 – ident: e_1_2_9_5_1 doi: 10.1016/j.cell.2020.03.045 – year: 2021 ident: e_1_2_9_19_1 article-title: Predicting the potential effect of E484K mutation on the binding of 28 antibodies to the spike protein of SARS‐CoV‐2 by molecular dynamics simulation and free energy calculation publication-title: ChemRxiv – ident: e_1_2_9_11_1 – ident: e_1_2_9_15_1 doi: 10.1038/d41586-021-01274-7 – ident: e_1_2_9_16_1 doi: 10.1016/j.micpath.2021.104831 |
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Emerged mutations can be attributed to increased transmissibility of the B.1.617 and B.1.36 Indian delta variants of SARS‐CoV‐2, most notably... Emerged mutations can be attributed to increased transmissibility of the B.1.617 and B.1.36 Indian delta variants of SARS-CoV-2, most notably substitutions... BackgroundEmerged mutations can be attributed to increased transmissibility of the B.1.617 and B.1.36 Indian delta variants of SARS‐CoV‐2, most notably... Binding assays using Biolayer Interferometry showed that the RBD containing L452R/E484Q present in the new SARS‐CoV‐2 variant B.1.617 interacts with ACE2 with... |
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| SubjectTerms | ACE2 Affinity Angiotensin-converting enzyme 2 Antibodies BNT162 Vaccine COVID-19 Enzyme-linked immunosorbent assay Humans Immune Evasion Immunoglobulin G mRNA mRNA Vaccines Mutants Mutation neutralization Original ORIGINAL ARTICLES Point mutation Protein Binding RBD SARS-CoV-2 Severe acute respiratory syndrome coronavirus 2 Spike Glycoprotein, Coronavirus - metabolism Titration Vaccination vaccine Vaccines, Synthetic |
| Title | In vitro data suggest that Indian delta variant B.1.617 of SARS‐CoV‐2 escapes neutralization by both receptor affinity and immune evasion |
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