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Broadly neutralizing and protective nanobodies against SARS-CoV-2 Omicron subvariants BA.1, BA.2, and BA.4/5 and diverse sarbecoviruses.

<div class='caption-title'>Phylogenetic, neutralizing, binding, and genetic properties of isolated nanobodies against SARS-CoV-2 and SARS-CoV-1.</div>
<div class='caption-title'>Classification and neutralizing activity of isolated nanobodies against SARS-CoV-2 variants and diverse hACE2-dependent sarbecoviruses.</div>
<div class='caption-title'>Crystal structures and epitope of three representative nanobodies bound to SARS-CoV-2 RBD or SARS-CoV-1 RBD.</div>
Li M, Ren Y, Aw ZQ, Chen B, Yang Z, Lei Y, Cheng L, Liang Q, Hong J, Yang Y, Chen J, Wong YH, Wei J, Shan S, Zhang S, Ge J, Wang R, Dong JZ, Chen Y, Shi X, Zhang Q, Zhang Z, Chu JJH, Wang X, Zhang L
OpenAccess logo Nat Commun 13 7957 (2022)
Related entries: 7x2j, 7x2k, 7x2m

Cited: 11 times
EuropePMC logo PMID: 36575191

Abstract

As SARS-CoV-2 Omicron and other variants of concern (VOCs) continue spreading worldwide, development of antibodies and vaccines to confer broad and protective activity is a global priority. Here, we report on the identification of a special group of nanobodies from immunized alpaca with potency against diverse VOCs including Omicron subvariants BA.1, BA.2 and BA.4/5, SARS-CoV-1, and major sarbecoviruses. Crystal structure analysis of one representative nanobody, 3-2A2-4, discovers a highly conserved epitope located between the cryptic and the outer face of the receptor binding domain (RBD), distinctive from the receptor ACE2 binding site. Cryo-EM and biochemical evaluation reveal that 3-2A2-4 interferes structural alteration of RBD required for ACE2 binding. Passive delivery of 3-2A2-4 protects K18-hACE2 mice from infection of authentic SARS-CoV-2 Delta and Omicron. Identification of these unique nanobodies will inform the development of next generation antibody therapies and design of pan-sarbecovirus vaccines.

Reviews citing this publication (3)

  1. Biomimetic Nanotechnology for SARS-CoV-2 Treatment. Li S, Liu X, Liu G, Liu C. Viruses 15 596 (2023)
  2. SARS-CoV-2 proteins structural studies using synchrotron radiation. Kosenko M, Onkhonova G, Susloparov I, Ryzhikov A. Biophys Rev 15 1185-1194 (2023)
  3. Streamlining spatial omics data analysis with Pysodb. Lin S, Zhao F, Wu Z, Yao J, Zhao Y, Yuan Z. Nat Protoc (2023)

Articles citing this publication (8)

  1. A broad-spectrum macrocyclic peptide inhibitor of the SARS-CoV-2 spike protein. Thijssen V, Hurdiss DL, Debski-Antoniak OJ, Spence MA, Franck C, Norman A, Aggarwal A, Mokiem NJ, van Dongen DAA, Vermeir SW, Liu M, Li W, Chatziandreou M, Donselaar T, Du W, Drulyte I, Bosch BJ, Snijder J, Turville SG, Payne RJ, Jackson CJ, van Kuppeveld FJM, Jongkees SAK. Proc Natl Acad Sci U S A 120 e2303292120 (2023)
  2. Infection with wild-type SARS-CoV-2 elicits broadly neutralizing and protective antibodies against omicron subvariants. Ju B, Zhang Q, Wang Z, Aw ZQ, Chen P, Zhou B, Wang R, Ge X, Lv Q, Cheng L, Zhang R, Wong YH, Chen H, Wang H, Shan S, Liao X, Shi X, Liu L, Chu JJH, Wang X, Zhang Z, Zhang L. Nat Immunol 24 690-699 (2023)
  3. Nanobodies with cross-neutralizing activity provide prominent therapeutic efficacy in mild and severe COVID-19 rodent models. Han Q, Wang S, Wang Z, Zhang C, Wang X, Feng N, Wang T, Zhao Y, Chi H, Yan F, Xia X. Virol Sin 38 787-800 (2023)
  4. Development of a bispecific nanobody conjugate broadly neutralizes diverse SARS-CoV-2 variants and structural basis for its broad neutralization. Yang J, Lin S, Chen Z, Yang F, Guo L, Wang L, Duan Y, Zhang X, Dai Y, Yin K, Yu C, Yuan X, Sun H, He B, Cao Y, Ye H, Dong H, Liu X, Chen B, Li J, Zhao Q, Lu G. PLoS Pathog 19 e1011804 (2023)
  5. Disulfide stabilization reveals conserved dynamic features between SARS-CoV-1 and SARS-CoV-2 spikes. Zhang X, Li Z, Zhang Y, Liu Y, Wang J, Liu B, Chen Q, Wang Q, Fu L, Wang P, Zhong X, Jin L, Yan Q, Chen L, He J, Zhao J, Xiong X. Life Sci Alliance 6 e202201796 (2023)
  6. Screening, Expression and Identification of Nanobody Against Monkeypox Virus A35R. Meng N, Cheng X, Sun M, Zhang Y, Sun X, Liu X, Chen J. Int J Nanomedicine 18 7173-7181 (2023)
  7. The 2nd China Vaccinology Integrated Innovation & Teaching Development Conference: Promoting the construction of vaccinology discipline system. Chen Y, Shu Y, Zheng H, Sun C, Fu C. Hum Vaccin Immunother 20 2300157 (2024)
  8. The cAMP receptor protein (CRP) enhances the competitive nature of Salmonella Typhimurium. Sawant K, Shashidhar R. Arch Microbiol 205 197 (2023)


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