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Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies.
<div class='caption-title'>Coronavirus S Proteins Show Localized Regions of Conservation and Variability</div>
<div class='caption-title'>Plasma Fabs Bind to SARS-CoV-2 S Protein</div>
Barnes CO, West AP, Huey-Tubman KE, Hoffmann MAG, Sharaf NG, Hoffman PR, Koranda N, Gristick HB, Gaebler C, Muecksch F, Lorenzi JCC, Finkin S, Hägglöf T, Hurley A, Millard KG, Weisblum Y, Schmidt F, Hatziioannou T, Bieniasz PD, Caskey M, Robbiani DF, Nussenzweig MC, Bjorkman PJ
OpenAccess logo Cell 182 828-842.e16 (2020)
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Cited: 468 times
EuropePMC logo PMID: 32645326

Abstract

Neutralizing antibody responses to coronaviruses mainly target the receptor-binding domain (RBD) of the trimeric spike. Here, we characterized polyclonal immunoglobulin Gs (IgGs) and Fabs from COVID-19 convalescent individuals for recognition of coronavirus spikes. Plasma IgGs differed in their focus on RBD epitopes, recognition of alpha- and beta-coronaviruses, and contributions of avidity to increased binding/neutralization of IgGs over Fabs. Using electron microscopy, we examined specificities of polyclonal plasma Fabs, revealing recognition of both S1A and RBD epitopes on SARS-CoV-2 spike. Moreover, a 3.4 Å cryo-electron microscopy (cryo-EM) structure of a neutralizing monoclonal Fab-spike complex revealed an epitope that blocks ACE2 receptor binding. Modeling based on these structures suggested different potentials for inter-spike crosslinking by IgGs on viruses, and characterized IgGs would not be affected by identified SARS-CoV-2 spike mutations. Overall, our studies structurally define a recurrent anti-SARS-CoV-2 antibody class derived from VH3-53/VH3-66 and similarity to a SARS-CoV VH3-30 antibody, providing criteria for evaluating vaccine-elicited antibodies.

Reviews - 6xcn mentioned but not cited (10)

  1. The SARS-CoV-2 Spike Glycoprotein as a Drug and Vaccine Target: Structural Insights into Its Complexes with ACE2 and Antibodies. Papageorgiou AC, Mohsin I. Cells 9 E2343 (2020)
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  4. Man-Specific, GalNAc/T/Tn-Specific and Neu5Ac-Specific Seaweed Lectins as Glycan Probes for the SARS-CoV-2 (COVID-19) Coronavirus. Barre A, Damme EJMV, Simplicien M, Benoist H, Rougé P. Mar Drugs 18 E543 (2020)
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Articles - 6xcn mentioned but not cited (33)

  1. Structures of Human Antibodies Bound to SARS-CoV-2 Spike Reveal Common Epitopes and Recurrent Features of Antibodies. Barnes CO, West AP, Huey-Tubman KE, Hoffmann MAG, Sharaf NG, Hoffman PR, Koranda N, Gristick HB, Gaebler C, Muecksch F, Lorenzi JCC, Finkin S, Hägglöf T, Hurley A, Millard KG, Weisblum Y, Schmidt F, Hatziioannou T, Bieniasz PD, Caskey M, Robbiani DF, Nussenzweig MC, Bjorkman PJ. Cell 182 828-842.e16 (2020)
  2. Mapping mutations to the SARS-CoV-2 RBD that escape binding by different classes of antibodies. Greaney AJ, Starr TN, Barnes CO, Weisblum Y, Schmidt F, Caskey M, Gaebler C, Cho A, Agudelo M, Finkin S, Wang Z, Poston D, Muecksch F, Hatziioannou T, Bieniasz PD, Robbiani DF, Nussenzweig MC, Bjorkman PJ, Bloom JD. Nat Commun 12 4196 (2021)
  3. Evolutionary analysis of the Delta and Delta Plus variants of the SARS-CoV-2 viruses. Kannan SR, Spratt AN, Cohen AR, Naqvi SH, Chand HS, Quinn TP, Lorson CL, Byrareddy SN, Singh K. J Autoimmun 124 102715 (2021)
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  5. Modular basis for potent SARS-CoV-2 neutralization by a prevalent VH1-2-derived antibody class. Rapp M, Guo Y, Reddem ER, Yu J, Liu L, Wang P, Cerutti G, Katsamba P, Bimela JS, Bahna FA, Mannepalli SM, Zhang B, Kwong PD, Huang Y, Ho DD, Shapiro L, Sheng Z. Cell Rep 35 108950 (2021)
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  10. Versatile and multivalent nanobodies efficiently neutralize SARS-CoV-2. Xiang Y, Nambulli S, Xiao Z, Liu H, Sang Z, Duprex WP, Schneidman-Duhovny D, Zhang C, Shi Y. Science 370 1479-1484 (2020)
  11. Elucidating important structural features for the binding affinity of spike - SARS-CoV-2 neutralizing antibody complexes. Sharma D, Rawat P, Janakiraman V, Gromiha MM. Proteins 90 824-834 (2022)
  12. The trispecific DARPin ensovibep inhibits diverse SARS-CoV-2 variants. Rothenberger S, Hurdiss DL, Walser M, Malvezzi F, Mayor J, Ryter S, Moreno H, Liechti N, Bosshart A, Iss C, Calabro V, Cornelius A, Hospodarsch T, Neculcea A, Looser T, Schlegel A, Fontaine S, Villemagne D, Paladino M, Schiegg D, Mangold S, Reichen C, Radom F, Kaufmann Y, Schaible D, Schlegel I, Zitt C, Sigrist G, Straumann M, Wolter J, Comby M, Sacarcelik F, Drulyte I, Lyoo H, Wang C, Li W, Du W, Binz HK, Herrup R, Lusvarghi S, Neerukonda SN, Vassell R, Wang W, Adler JM, Eschke K, Nascimento M, Abdelgawad A, Gruber AD, Bushe J, Kershaw O, Knutson CG, Balavenkatraman KK, Ramanathan K, Wyler E, Teixeira Alves LG, Lewis S, Watson R, Haeuptle MA, Zürcher A, Dawson KM, Steiner D, Weiss CD, Amstutz P, van Kuppeveld FJM, Stumpp MT, Bosch BJ, Engler O, Trimpert J. Nat Biotechnol 40 1845-1854 (2022)
  13. Dynamic Interactions of Fully Glycosylated SARS-CoV-2 Spike Protein with Various Antibodies. Cao Y, Choi YK, Frank M, Woo H, Park SJ, Yeom MS, Seok C, Im W. J Chem Theory Comput 17 6559-6569 (2021)
  14. research-article A broadly neutralizing antibody protects against SARS-CoV, pre-emergent bat CoVs, and SARS-CoV-2 variants in mice. Martinez DR, Schaefer A, Gobeil S, Li D, De la Cruz G, Parks R, Lu X, Barr M, Manne K, Mansouri K, Edwards RJ, Yount B, Anasti K, Montgomery SA, Shen S, Zhou T, Kwong PD, Graham BS, Mascola JR, Montefiori DC, Alam M, Sempowski GD, Wiehe K, Saunders KO, Acharya P, Haynes BF, Baric RS. bioRxiv 2021.04.27.441655 (2021)
  15. research-article A monoclonal antibody against staphylococcal enterotoxin B superantigen inhibits SARS-CoV-2 entry in vitro. Cheng MH, Porritt RA, Rivas MN, Krieger JM, Ozdemir AB, Garcia G, Arumugaswami V, Fries BC, Arditi M, Bahar I. bioRxiv 2020.11.24.395079 (2020)
  16. Impact of new variants on SARS-CoV-2 infectivity and neutralization: A molecular assessment of the alterations in the spike-host protein interactions. Cheng MH, Krieger JM, Banerjee A, Xiang Y, Kaynak B, Shi Y, Arditi M, Bahar I. iScience 25 103939 (2022)
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  23. research-article Dynamic Interactions of Fully Glycosylated SARS-CoV-2 Spike Protein with Various Antibodies. Cao Y, Choi YK, Frank M, Woo H, Park SJ, Yeom MS, Seok C, Im W. bioRxiv 2021.05.10.443519 (2021)
  24. Human inhalable antibody fragments neutralizing SARS-CoV-2 variants for COVID-19 therapy. Minenkova O, Santapaola D, Milazzo FM, Anastasi AM, Battistuzzi G, Chiapparino C, Rosi A, Gritti G, Borleri G, Rambaldi A, Dental C, Viollet C, Pagano B, Salvini L, Marra E, Luberto L, Rossi A, Riccio A, Merlo Pich E, Santoro MG, De Santis R. Mol Ther 30 1979-1993 (2022)
  25. Immunity evasion: consequence of the N501Y mutation of the SARS-CoV-2 spike glycoprotein. Uzoeto HO, Ajima JN, Arazu AV, Ibiang GO, Cosmas S, Durojaye OA. J Genet Eng Biotechnol 20 10 (2022)
  26. MutCov: A pipeline for evaluating the effect of mutations in spike protein on infectivity and antigenicity of SARS-CoV-2. Zhou W, Xu C, Luo M, Wang P, Xu Z, Xue G, Jin X, Huang Y, Li Y, Nie H, Jiang Q, Anashkina AA. Comput Biol Med 145 105509 (2022)
  27. research-article Mutational escape from the polyclonal antibody response to SARS-CoV-2 infection is largely shaped by a single class of antibodies. Greaney AJ, Starr TN, Barnes CO, Weisblum Y, Schmidt F, Caskey M, Gaebler C, Cho A, Agudelo M, Finkin S, Wang Z, Poston D, Muecksch F, Hatziioannou T, Bieniasz PD, Robbiani DF, Nussenzweig MC, Bjorkman PJ, Bloom JD. bioRxiv 2021.03.17.435863 (2021)
  28. research-article Structural models of SARS-CoV-2 Omicron variant in complex with ACE2 receptor or antibodies suggest altered binding interfaces. Lubin JH, Markosian C, Balamurugan D, Pasqualini R, Arap W, Burley SK, Khare SD. bioRxiv 2021.12.12.472313 (2021)
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  33. research-article Versatile, Multivalent Nanobody Cocktails Efficiently Neutralize SARS-CoV-2. Xiang Y, Nambulli S, Xiao Z, Liu H, Sang Z, Duprex WP, Schneidman-Duhovny D, Zhang C, Shi Y. bioRxiv 2020.08.24.264333 (2020)


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