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Selection, biophysical and structural analysis of synthetic nanobodies that effectively neutralize SARS-CoV-2.

<div class='caption-title'>Selection of sybodies against SARS-CoV-2 RBD.</div>
<div class='caption-title'>Biophysical characterization of identified sybodies.</div>
<div class='caption-title'>Sb23 neutralizes SARS-CoV-2 pseudoviruses and competes with ACE2.</div>
Custódio TF, Das H, Sheward DJ, Hanke L, Pazicky S, Pieprzyk J, Sorgenfrei M, Schroer MA, Gruzinov AY, Jeffries CM, Graewert MA, Svergun DI, Dobrev N, Remans K, Seeger MA, McInerney GM, Murrell B, Hällberg BM, Löw C
OpenAccess logo Nat Commun 11 5588 (2020)
Cited: 102 times
EuropePMC logo PMID: 33149112

Abstract

The coronavirus SARS-CoV-2 is the cause of the ongoing COVID-19 pandemic. Therapeutic neutralizing antibodies constitute a key short-to-medium term approach to tackle COVID-19. However, traditional antibody production is hampered by long development times and costly production. Here, we report the rapid isolation and characterization of nanobodies from a synthetic library, known as sybodies (Sb), that target the receptor-binding domain (RBD) of the SARS-CoV-2 spike protein. Several binders with low nanomolar affinities and efficient neutralization activity were identified of which Sb23 displayed high affinity and neutralized pseudovirus with an IC50 of 0.6 µg/ml. A cryo-EM structure of the spike bound to Sb23 showed that Sb23 binds competitively in the ACE2 binding site. Furthermore, the cryo-EM reconstruction revealed an unusual conformation of the spike where two RBDs are in the 'up' ACE2-binding conformation. The combined approach represents an alternative, fast workflow to select binders with neutralizing activity against newly emerging viruses.

Reviews - 7a29 mentioned but not cited (4)

  1. Monoclonal antibody therapies against SARS-CoV-2. Focosi D, McConnell S, Casadevall A, Cappello E, Valdiserra G, Tuccori M. Lancet Infect Dis 22 e311-e326 (2022)
  2. Integrative overview of antibodies against SARS-CoV-2 and their possible applications in COVID-19 prophylaxis and treatment. Valdez-Cruz NA, García-Hernández E, Espitia C, Cobos-Marín L, Altamirano C, Bando-Campos CG, Cofas-Vargas LF, Coronado-Aceves EW, González-Hernández RA, Hernández-Peralta P, Juárez-López D, Ortega-Portilla PA, Restrepo-Pineda S, Zelada-Cordero P, Trujillo-Roldán MA. Microb Cell Fact 20 88 (2021)
  3. Recent advances in nanotechnology-based COVID-19 vaccines and therapeutic antibodies. Du L, Yang Y, Zhang X, Li F. Nanoscale 14 1054-1074 (2022)
  4. Structural Biology of Nanobodies against the Spike Protein of SARS-CoV-2. Tang Q, Owens RJ, Naismith JH. Viruses 13 2214 (2021)

Articles - 7a29 mentioned but not cited (13)

  1. Selection, biophysical and structural analysis of synthetic nanobodies that effectively neutralize SARS-CoV-2. Custódio TF, Das H, Sheward DJ, Hanke L, Pazicky S, Pieprzyk J, Sorgenfrei M, Schroer MA, Gruzinov AY, Jeffries CM, Graewert MA, Svergun DI, Dobrev N, Remans K, Seeger MA, McInerney GM, Murrell B, Hällberg BM, Löw C. Nat Commun 11 5588 (2020)
  2. Prediction and mitigation of mutation threats to COVID-19 vaccines and antibody therapies. Chen J, Gao K, Wang R, Wei GW. Chem Sci 12 6929-6948 (2021)
  3. Potent neutralizing nanobodies resist convergent circulating variants of SARS-CoV-2 by targeting diverse and conserved epitopes. Sun D, Sang Z, Kim YJ, Xiang Y, Cohen T, Belford AK, Huet A, Conway JF, Sun J, Taylor DJ, Schneidman-Duhovny D, Zhang C, Huang W, Shi Y. Nat Commun 12 4676 (2021)
  4. Biparatopic sybodies neutralize SARS-CoV-2 variants of concern and mitigate drug resistance. Walter JD, Scherer M, Hutter CAJ, Garaeva AA, Zimmermann I, Wyss M, Rheinberger J, Ruedin Y, Earp JC, Egloff P, Sorgenfrei M, Hürlimann LM, Gonda I, Meier G, Remm S, Thavarasah S, van Geest G, Bruggmann R, Zimmer G, Slotboom DJ, Paulino C, Plattet P, Seeger MA. EMBO Rep 23 e54199 (2022)
  5. An ultrapotent pan-β-coronavirus lineage B (β-CoV-B) neutralizing antibody locks the receptor-binding domain in closed conformation by targeting its conserved epitope. Liu Z, Xu W, Chen Z, Fu W, Zhan W, Gao Y, Zhou J, Zhou Y, Wu J, Wang Q, Zhang X, Hao A, Wu W, Zhang Q, Li Y, Fan K, Chen R, Jiang Q, Mayer CT, Schoofs T, Xie Y, Jiang S, Wen Y, Yuan Z, Wang K, Lu L, Sun L, Wang Q. Protein Cell 13 655-675 (2022)
  6. Structure and Mutations of SARS-CoV-2 Spike Protein: A Focused Overview. Mehra R, Kepp KP. ACS Infect Dis 8 29-58 (2022)
  7. Analysis of SARS-CoV-2 Genomes from West Java, Indonesia. Fibriani A, Stephanie R, Alfiantie AA, Siregar ALF, Pradani GAP, Yamahoki N, Purba WS, Alamanda CNC, Rahmawati E, Rachman RW, Robiani R, Ristandi RB. Viruses 13 2097 (2021)
  8. Structural basis of broad SARS-CoV-2 cross-neutralization by affinity-matured public antibodies. Sheward DJ, Pushparaj P, Das H, Greaney AJ, Kim C, Kim S, Hanke L, Hyllner E, Dyrdak R, Lee J, Dopico XC, Dosenovic P, Peacock TP, McInerney GM, Albert J, Corcoran M, Bloom JD, Murrell B, Karlsson Hedestam GB, Hällberg BM. Cell Rep Med 5 101577 (2024)
  9. Immunoglobulin germline gene polymorphisms influence the function of SARS-CoV-2 neutralizing antibodies. Pushparaj P, Nicoletto A, Sheward DJ, Das H, Castro Dopico X, Perez Vidakovics L, Hanke L, Chernyshev M, Narang S, Kim S, Fischbach J, Ekström S, McInerney G, Hällberg BM, Murrell B, Corcoran M, Karlsson Hedestam GB. Immunity 56 193-206.e7 (2023)
  10. Comprehensive structural analysis reveals broad-spectrum neutralizing antibodies against SARS-CoV-2 Omicron variants. Chi X, Xia L, Zhang G, Chi X, Huang B, Zhang Y, Chen Z, Han J, Wu L, Li Z, Sun H, Huang P, Yu C, Chen W, Zhou Q. Cell Discov 9 37 (2023)
  11. 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)
  12. Nanobody engineering for SARS-CoV-2 neutralization and detection. Hannula L, Kuivanen S, Lasham J, Kant R, Kareinen L, Bogacheva M, Strandin T, Sironen T, Hepojoki J, Sharma V, Saviranta P, Kipar A, Vapalahti O, Huiskonen JT, Rissanen I. Microbiol Spectr 12 e0419922 (2024)
  13. research-article Potent neutralizing nanobodies resist convergent circulating variants of SARS-CoV-2 by targeting novel and conserved epitopes. Sun D, Sang Z, Kim YJ, Xiang Y, Cohen T, Belford AK, Huet A, Conway JF, Sun J, Taylor DJ, Schneidman-Duhovny D, Zhang C, Huang W, Shi Y. bioRxiv 2021.03.09.434592 (2021)


Reviews citing this publication (31)

  1. SARS-CoV-2 Antiviral Therapy. Tao K, Tzou PL, Nouhin J, Bonilla H, Jagannathan P, Shafer RW. Clin Microbiol Rev 34 e0010921 (2021)
  2. Structural Analysis of Neutralizing Epitopes of the SARS-CoV-2 Spike to Guide Therapy and Vaccine Design Strategies. Finkelstein MT, Mermelstein AG, Parker Miller E, Seth PC, Stancofski ED, Fera D. Viruses 13 134 (2021)
  3. Camelid Single-Domain Antibodies: Promises and Challenges as Lifesaving Treatments. Arbabi-Ghahroudi M. Int J Mol Sci 23 5009 (2022)
  4. Recent review of COVID-19 management: diagnosis, treatment and vaccination. Chavda VP, Vuppu S, Mishra T, Kamaraj S, Patel AB, Sharma N, Chen ZS. Pharmacol Rep 74 1120-1148 (2022)
  5. Prospects of Neutralizing Nanobodies Against SARS-CoV-2. Chen F, Liu Z, Jiang F. Front Immunol 12 690742 (2021)
  6. SARS-CoV-2-neutralising monoclonal antibodies to prevent COVID-19. Hirsch C, Park YS, Piechotta V, Chai KL, Estcourt LJ, Monsef I, Salomon S, Wood EM, So-Osman C, McQuilten Z, Spinner CD, Malin JJ, Stegemann M, Skoetz N, Kreuzberger N. Cochrane Database Syst Rev 6 CD014945 (2022)
  7. Perspective on therapeutic and diagnostic potential of camel nanobodies for coronavirus disease-19 (COVID-19). Bessalah S, Jebahi S, Mejri N, Salhi I, Khorchani T, Hammadi M. 3 Biotech 11 89 (2021)
  8. Bovine-derived antibodies and camelid-derived nanobodies as biotherapeutic weapons against SARS-CoV-2 and its variants: A review article. Saied AA, Metwally AA, Alobo M, Shah J, Sharun K, Dhama K. Int J Surg 98 106233 (2022)
  9. Targeting the SARS-CoV-2-spike protein: from antibodies to miniproteins and peptides. Pomplun S. RSC Med Chem 12 197-202 (2020)
  10. Potent Molecular Feature-based Neutralizing Monoclonal Antibodies as Promising Therapeutics Against SARS-CoV-2 Infection. Kombe Kombe AJ, Zahid A, Mohammed A, Shi R, Jin T. Front Mol Biosci 8 670815 (2021)
  11. The role and uses of antibodies in COVID-19 infections: a living review. Scourfield DO, Reed SG, Quastel M, Alderson J, Bart VMT, Teijeira Crespo A, Jones R, Pring E, Richter FC, Oxford-Cardiff COVID-19 Literature Consortium , Burnell SEA. Oxf Open Immunol 2 iqab003 (2021)
  12. 50 Years of structural immunology. Wilson IA, Stanfield RL. J Biol Chem 296 100745 (2021)
  13. Anti-SARS-CoV-1 and -2 nanobody engineering towards avidity-inspired therapeutics. Obeng EM, Dzuvor CKO, Danquah MK. Nano Today 42 101350 (2022)
  14. The development of neutralizing antibodies against SARS-CoV-2 and their common features. Liu LD, Lian C, Yeap LS, Meng FL. J Mol Cell Biol 12 980-986 (2020)
  15. Advances in Nanomaterial-Based Platforms to Combat COVID-19: Diagnostics, Preventions, Therapeutics, and Vaccine Developments. Mahmud N, Anik MI, Hossain MK, Khan MI, Uddin S, Ashrafuzzaman M, Rahaman MM. ACS Appl Bio Mater 5 2431-2460 (2022)
  16. Analysis of the molecular mechanism of SARS-CoV-2 antibodies. Jin D, Wei J, Sun J. Biochem Biophys Res Commun 566 45-52 (2021)
  17. Nanobodies as powerful pulmonary targeted biotherapeutics against SARS-CoV-2, pharmaceutical point of view. Najmeddin A, Bahrololoumi Shapourabadi M, Behdani M, Dorkoosh F. Biochim Biophys Acta Gen Subj 1865 129974 (2021)
  18. The role of single-domain antibodies (or nanobodies) in SARS-CoV-2 neutralization. Zebardast A, Hosseini P, Hasanzadeh A, Latifi T. Mol Biol Rep 49 647-656 (2022)
  19. The Potential of Nanobodies for COVID-19 Diagnostics and Therapeutics. Naidoo DB, Chuturgoon AA. Mol Diagn Ther 27 193-226 (2023)
  20. Therapeutic applications of nanobodies against SARS-CoV-2 and other viral infections: Current update. Bhattacharya M, Chatterjee S, Lee SS, Chakraborty C. Int J Biol Macromol 229 70-80 (2023)
  21. Advanced microscopy technologies enable rapid response to SARS-CoV-2 pandemic. Cortese M, Laketa V. Cell Microbiol 23 e13319 (2021)
  22. Emerging Landscape of Nanobodies and Their Neutralizing Applications against SARS-CoV-2 Virus. Feng X, Wang H. ACS Pharmacol Transl Sci 6 925-942 (2023)
  23. Single-Domain Antibodies as Therapeutics for Respiratory RNA Virus Infections. Huang K, Ying T, Wu Y. Viruses 14 1162 (2022)
  24. Nanotechnology-based approaches in the fight against SARS-CoV-2. Albaz AA, Rafeeq MM, Sain ZM, Almutairi WA, Alamri AS, Aloufi AH, Almalki WH, Tarique M. AIMS Microbiol 7 368-398 (2021)
  25. Native, engineered and de novo designed ligands targeting the SARS-CoV-2 spike protein. Costa CFS, Barbosa AJM, Dias AMGC, Roque ACA. Biotechnol Adv 59 107986 (2022)
  26. Applications of nanobodies in the prevention, detection, and treatment of the evolving SARS-CoV-2. Wang W, Hu Y, Li B, Wang H, Shen J. Biochem Pharmacol 208 115401 (2023)
  27. Epitope Analysis of Anti-SARS-CoV-2 Neutralizing Antibodies. Xue JB, Tao SC. Curr Med Sci 41 1065-1074 (2021)
  28. Multi-omics for COVID-19: driving development of therapeutics and vaccines. Guo M, Xiong M, Peng J, Guan T, Su H, Huang Y, Yang CG, Li Y, Boraschi D, Pillaiyar T, Wang G, Yi C, Xu Y, Chen C. Natl Sci Rev 10 nwad161 (2023)
  29. Nanobodies in the fight against infectious diseases: repurposing nature's tiny weapons. Rizk SS, Moustafa DM, ElBanna SA, Nour El-Din HT, Attia AS. World J Microbiol Biotechnol 40 209 (2024)
  30. Single domain antibodies derived from ancient animals as broadly neutralizing agents for SARS-CoV-2 and other coronaviruses. Lim HT, Kok BH, Lim CP, Abdul Majeed AB, Leow CY, Leow CH. Biomed Eng Adv 4 100054 (2022)
  31. Single domain antibodies from camelids in the treatment of microbial infections. De Greve H, Fioravanti A. Front Immunol 15 1334829 (2024)

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  1. Structure-guided multivalent nanobodies block SARS-CoV-2 infection and suppress mutational escape. Koenig PA, Das H, Liu H, Kümmerer BM, Gohr FN, Jenster LM, Schiffelers LDJ, Tesfamariam YM, Uchima M, Wuerth JD, Gatterdam K, Ruetalo N, Christensen MH, Fandrey CI, Normann S, Tödtmann JMP, Pritzl S, Hanke L, Boos J, Yuan M, Zhu X, Schmid-Burgk JL, Kato H, Schindler M, Wilson IA, Geyer M, Ludwig KU, Hällberg BM, Wu NC, Schmidt FI. Science 371 eabe6230 (2021)
  2. 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)
  3. Linear epitope landscape of the SARS-CoV-2 Spike protein constructed from 1,051 COVID-19 patients. Li Y, Ma ML, Lei Q, Wang F, Hong W, Lai DY, Hou H, Xu ZW, Zhang B, Chen H, Yu C, Xue JB, Zheng YX, Wang XN, Jiang HW, Zhang HN, Qi H, Guo SJ, Zhang Y, Lin X, Yao Z, Wu J, Sheng H, Zhang Y, Wei H, Sun Z, Fan X, Tao SC. Cell Rep 34 108915 (2021)
  4. Inhalable Nanobody (PiN-21) prevents and treats SARS-CoV-2 infections in Syrian hamsters at ultra-low doses. Nambulli S, Xiang Y, Tilston-Lunel NL, Rennick LJ, Sang Z, Klimstra WB, Reed DS, Crossland NA, Shi Y, Duprex WP. Sci Adv 7 eabh0319 (2021)
  5. Nanobody cocktails potently neutralize SARS-CoV-2 D614G N501Y variant and protect mice. Pymm P, Adair A, Chan LJ, Cooney JP, Mordant FL, Allison CC, Lopez E, Haycroft ER, O'Neill MT, Tan LL, Dietrich MH, Drew D, Doerflinger M, Dengler MA, Scott NE, Wheatley AK, Gherardin NA, Venugopal H, Cromer D, Davenport MP, Pickering R, Godfrey DI, Purcell DFJ, Kent SJ, Chung AW, Subbarao K, Pellegrini M, Glukhova A, Tham WH. Proc Natl Acad Sci U S A 118 e2101918118 (2021)
  6. A potent SARS-CoV-2 neutralising nanobody shows therapeutic efficacy in the Syrian golden hamster model of COVID-19. Huo J, Mikolajek H, Le Bas A, Clark JJ, Sharma P, Kipar A, Dormon J, Norman C, Weckener M, Clare DK, Harrison PJ, Tree JA, Buttigieg KR, Salguero FJ, Watson R, Knott D, Carnell O, Ngabo D, Elmore MJ, Fotheringham S, Harding A, Moynié L, Ward PN, Dumoux M, Prince T, Hall Y, Hiscox JA, Owen A, James W, Carroll MW, Stewart JP, Naismith JH, Owens RJ. Nat Commun 12 5469 (2021)
  7. High affinity nanobodies block SARS-CoV-2 spike receptor binding domain interaction with human angiotensin converting enzyme. Esparza TJ, Martin NP, Anderson GP, Goldman ER, Brody DL. Sci Rep 10 22370 (2020)
  8. A potent neutralizing nanobody against SARS-CoV-2 with inhaled delivery potential. Gai J, Ma L, Li G, Zhu M, Qiao P, Li X, Zhang H, Zhang Y, Chen Y, Ji W, Zhang H, Cao H, Li X, Gong R, Wan Y. MedComm (2020) 2 101-113 (2021)
  9. A synthetic nanobody targeting RBD protects hamsters from SARS-CoV-2 infection. Li T, Cai H, Yao H, Zhou B, Zhang N, van Vlissingen MF, Kuiken T, Han W, GeurtsvanKessel CH, Gong Y, Zhao Y, Shen Q, Qin W, Tian XX, Peng C, Lai Y, Wang Y, Hutter CAJ, Kuo SM, Bao J, Liu C, Wang Y, Richard AS, Raoul H, Lan J, Seeger MA, Cong Y, Rockx B, Wong G, Bi Y, Lavillette D, Li D. Nat Commun 12 4635 (2021)
  10. Neutralization of SARS-CoV-2 by highly potent, hyperthermostable, and mutation-tolerant nanobodies. Güttler T, Aksu M, Dickmanns A, Stegmann KM, Gregor K, Rees R, Taxer W, Rymarenko O, Schünemann J, Dienemann C, Gunkel P, Mussil B, Krull J, Teichmann U, Groß U, Cordes VC, Dobbelstein M, Görlich D. EMBO J 40 e107985 (2021)
  11. A bispecific monomeric nanobody induces spike trimer dimers and neutralizes SARS-CoV-2 in vivo. Hanke L, Das H, Sheward DJ, Perez Vidakovics L, Urgard E, Moliner-Morro A, Kim C, Karl V, Pankow A, Smith NL, Porebski B, Fernandez-Capetillo O, Sezgin E, Pedersen GK, Coquet JM, Hällberg BM, Murrell B, McInerney GM. Nat Commun 13 155 (2022)
  12. Potent Neutralization of SARS-CoV-2 by Hetero-bivalent Alpaca Nanobodies Targeting the Spike Receptor-Binding Domain. Ma H, Zeng W, Meng X, Huang X, Yang Y, Zhao D, Zhou P, Wang X, Zhao C, Sun Y, Wang P, Ou H, Hu X, Xiang Y, Jin T. J Virol 95 JVI.02438-20 (2021)
  13. Cross-neutralizing antibodies bind a SARS-CoV-2 cryptic site and resist circulating variants. Li T, Xue W, Zheng Q, Song S, Yang C, Xiong H, Zhang S, Hong M, Zhang Y, Yu H, Zhang Y, Sun H, Huang Y, Deng T, Chi X, Li J, Wang S, Zhou L, Chen T, Wang Y, Cheng T, Zhang T, Yuan Q, Zhao Q, Zhang J, McLellan JS, Zhou ZH, Zhang Z, Li S, Gu Y, Xia N. Nat Commun 12 5652 (2021)
  14. Highly synergistic combinations of nanobodies that target SARS-CoV-2 and are resistant to escape. Mast FD, Fridy PC, Ketaren NE, Wang J, Jacobs EY, Olivier JP, Sanyal T, Molloy KR, Schmidt F, Rutkowska M, Weisblum Y, Rich LM, Vanderwall ER, Dambrauskas N, Vigdorovich V, Keegan S, Jiler JB, Stein ME, Olinares PDB, Herlands L, Hatziioannou T, Sather DN, Debley JS, Fenyö D, Sali A, Bieniasz PD, Aitchison JD, Chait BT, Rout MP. Elife 10 e73027 (2021)
  15. NeutrobodyPlex-monitoring SARS-CoV-2 neutralizing immune responses using nanobodies. Wagner TR, Ostertag E, Kaiser PD, Gramlich M, Ruetalo N, Junker D, Haering J, Traenkle B, Becker M, Dulovic A, Schweizer H, Nueske S, Scholz A, Zeck A, Schenke-Layland K, Nelde A, Strengert M, Walz JS, Zocher G, Stehle T, Schindler M, Schneiderhan-Marra N, Rothbauer U. EMBO Rep 22 e52325 (2021)
  16. A high-affinity RBD-targeting nanobody improves fusion partner's potency against SARS-CoV-2. Yao H, Cai H, Li T, Zhou B, Qin W, Lavillette D, Li D. PLoS Pathog 17 e1009328 (2021)
  17. Directed evolution of potent neutralizing nanobodies against SARS-CoV-2 using CDR-swapping mutagenesis. Zupancic JM, Desai AA, Schardt JS, Pornnoppadol G, Makowski EK, Smith MD, Kennedy AA, Garcia de Mattos Barbosa M, Cascalho M, Lanigan TM, Tai AW, Tessier PM. Cell Chem Biol 28 1379-1388.e7 (2021)
  18. Nasal delivery of single-domain antibody improves symptoms of SARS-CoV-2 infection in an animal model. Haga K, Takai-Todaka R, Matsumura Y, Song C, Takano T, Tojo T, Nagami A, Ishida Y, Masaki H, Tsuchiya M, Ebisudani T, Sugimoto S, Sato T, Yasuda H, Fukunaga K, Sawada A, Nemoto N, Murata K, Morimoto T, Katayama K. PLoS Pathog 17 e1009542 (2021)
  19. Structures of synthetic nanobody-SARS-CoV-2 receptor-binding domain complexes reveal distinct sites of interaction. Ahmad J, Jiang J, Boyd LF, Zeher A, Huang R, Xia D, Natarajan K, Margulies DH. J Biol Chem 297 101202 (2021)
  20. Engineered Multivalent Nanobodies Potently and Broadly Neutralize SARS-CoV-2 Variants. Zupancic JM, Schardt JS, Desai AA, Makowski EK, Smith MD, Pornnoppadol G, Garcia de Mattos Barbosa M, Cascalho M, Lanigan TM, Tessier PM. Adv Ther (Weinh) 4 2100099 (2021)
  21. Outlook of therapeutic and diagnostic competency of nanobodies against SARS-CoV-2: A systematic review. Aria H, Mahmoodi F, Ghaheh HS, Faranak Mavandadnejad, Zare H, Heiat M, Bakherad H. Anal Biochem 640 114546 (2022)
  22. Arsenal of nanobodies shows broad-spectrum neutralization against SARS-CoV-2 variants of concern in vitro and in vivo in hamster models. Rossotti MA, van Faassen H, Tran AT, Sheff J, Sandhu JK, Duque D, Hewitt M, Wen X, Bavananthasivam J, Beitari S, Matte K, Laroche G, Giguère PM, Gervais C, Stuible M, Guimond J, Perret S, Hussack G, Langlois MA, Durocher Y, Tanha J. Commun Biol 5 933 (2022)
  23. Hetero-bivalent nanobodies provide broad-spectrum protection against SARS-CoV-2 variants of concern including Omicron. Ma H, Zhang X, Zheng P, Dube PH, Zeng W, Chen S, Cheng Q, Yang Y, Wu Y, Zhou J, Hu X, Xiang Y, Zhang H, Chiu S, Jin T. Cell Res 32 831-842 (2022)
  24. Structure-guided antibody cocktail for prevention and treatment of COVID-19. Su SC, Yang TJ, Yu PY, Liang KH, Chen WY, Yang CW, Lin HT, Wang MJ, Lu RM, Tso HC, Chung MJ, Hsieh TY, Chang YL, Lin SC, Hsu FY, Ke FY, Wu YH, Hwang YC, Liu IJ, Liang JJ, Liao CC, Ko HY, Sun CP, Wu PY, Jan JT, Chang YC, Lin YL, Tao MH, Hsu SD, Wu HC. PLoS Pathog 17 e1009704 (2021)
  25. A potent synthetic nanobody with broad-spectrum activity neutralizes SARS-CoV-2 virus and the Omicron variant BA.1 through a unique binding mode. Zhao D, Liu L, Liu X, Zhang J, Yin Y, Luan L, Jiang D, Yang X, Li L, Xiong H, Xing D, Zheng Q, Xia N, Tao Y, Li S, Huang H. J Nanobiotechnology 20 411 (2022)
  26. Nanomechanical sensor for rapid and ultrasensitive detection of tumor markers in serum using nanobody. Rao D, Mei K, Yan T, Wang Y, Wu W, Chen Y, Wang J, Zhang Q, Wu S. Nano Res 15 1003-1012 (2022)
  27. Trimeric receptor-binding domain of SARS-CoV-2 acts as a potent inhibitor of ACE2 receptor-mediated viral entry. Basavarajappa SC, Liu AR, Bruchez A, Li Z, Suzart VG, Liu Z, Chen Y, Xiao TS, Buck M, Ramakrishnan P. iScience 25 104716 (2022)
  28. 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)
  29. Binding Mechanism of Neutralizing Nanobodies Targeting SARS-CoV-2 Spike Glycoprotein. Golcuk M, Hacisuleyman A, Erman B, Yildiz A, Gur M. J Chem Inf Model 61 5152-5160 (2021)
  30. COVID-19: disease, or no disease? - that is the question. It's the dose stupid! Sehrawat S, Rouse BT. Microbes Infect 23 104779 (2021)
  31. Deamidation drives molecular aging of the SARS-CoV-2 spike protein receptor-binding motif. Lorenzo R, Defelipe LA, Aliperti L, Niebling S, Custódio TF, Löw C, Schwarz JJ, Remans K, Craig PO, Otero LH, Klinke S, García-Alai M, Sánchez IE, Alonso LG. J Biol Chem 297 101175 (2021)
  32. Modeling coronavirus spike protein dynamics: implications for immunogenicity and immune escape. Kunkel G, Madani M, White SJ, Verardi PH, Tarakanova A. Biophys J 120 5592-5618 (2021)
  33. Molecular basis of TASL recruitment by the peptide/histidine transporter 1, PHT1. Custódio TF, Killer M, Yu D, Puente V, Teufel DP, Pautsch A, Schnapp G, Grundl M, Kosinski J, Löw C. Nat Commun 14 5696 (2023)
  34. Nanobody derived using a peptide epitope from the spike protein receptor-binding motif inhibits entry of SARS-CoV-2 variants. Mendon N, Ganie RA, Kesarwani S, Dileep D, Sasi S, Lama P, Chandra A, Sirajuddin M. J Biol Chem 299 102732 (2023)
  35. Intranasal trimeric sherpabody inhibits SARS-CoV-2 including recent immunoevasive Omicron subvariants. Mäkelä AR, Uğurlu H, Hannula L, Kant R, Salminen P, Fagerlund R, Mäki S, Haveri A, Strandin T, Kareinen L, Hepojoki J, Kuivanen S, Levanov L, Pasternack A, Naves RA, Ritvos O, Österlund P, Sironen T, Vapalahti O, Kipar A, Huiskonen JT, Rissanen I, Saksela K. Nat Commun 14 1637 (2023)
  36. Nanobody-peptide-conjugate (NPC) for passive immunotherapy against SARS-CoV-2 variants of concern (VoC): a prospective pan-coronavirus therapeutics. Panda M, Kalita E, Singh S, Kumar K, Prajapati VK. Mol Divers 27 2577-2603 (2023)
  37. Biparatopic nanobodies targeting the receptor binding domain efficiently neutralize SARS-CoV-2. Pymm P, Redmond SJ, Dolezal O, Mordant F, Lopez E, Cooney JP, Davidson KC, Haycroft ER, Tan CW, Seneviratna R, Grimley SL, Purcell DFJ, Kent SJ, Wheatley AK, Wang LF, Leis A, Glukhova A, Pellegrini M, Chung AW, Subbarao K, Uldrich AP, Tham WH, Godfrey DI, Gherardin NA. iScience 25 105259 (2022)
  38. Implementing a method for engineering multivalency to substantially enhance binding of clinical trial anti-SARS-CoV-2 antibodies to wildtype spike and variants of concern proteins. Leach A, Miller A, Bentley E, Mattiuzzo G, Thomas J, McAndrew C, Van Montfort R, Rabbitts T. Sci Rep 11 10475 (2021)
  39. Measuring the Radius of Gyration and Intrinsic Flexibility of Viral Proteins in Buffer Solution Using Small-Angle X-ray Scattering. Funari R, Bhalla N, Gentile L. ACS Meas Sci Au 2 547-552 (2022)
  40. 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)
  41. Structural Characterization of a Neutralizing Nanobody With Broad Activity Against SARS-CoV-2 Variants. Li T, Zhou B, Luo Z, Lai Y, Huang S, Zhou Y, Li Y, Gautam A, Bourgeau S, Wang S, Bao J, Tan J, Lavillette D, Li D. Front Microbiol 13 875840 (2022)
  42. The synchrotron radiation source PETRA III and its future ultra-low-emittance upgrade PETRA IV. Schroer CG, Wille HC, Seeck OH, Bagschik K, Schulte-Schrepping H, Tischer M, Graafsma H, Laasch W, Baev K, Klumpp S, Bartolini R, Reichert H, Leemans W, Weckert E. Eur Phys J Plus 137 1312 (2022)
  43. A novel silk fibroin protein-based fusion system for enhancing the expression of nanobodies in Escherichia coli. Yu J, Guo Y, Gu Y, Fan X, Li F, Song H, Nian R, Liu W. Appl Microbiol Biotechnol 106 1967-1977 (2022)
  44. Research Support, N.I.H., Intramural Long-COVID: Phase 2 of the COVID-19 Pandemic. Goetzl EJ, Kapogiannis D. Am J Med 135 1277-1279 (2022)
  45. Recombinant Protein Micelles to Block Transduction by SARS-CoV-2 Pseudovirus. Chattaraj R, Kim CY, Lee D, Hammer DA. ACS Nano 16 17466-17477 (2022)
  46. Chimeric nanobody-decorated liposomes by self-assembly. Rahman MM, Wang J, Wang G, Su Z, Li Y, Chen Y, Meng J, Yao Y, Wang L, Wilkens S, Tan J, Luo J, Zhang T, Zhu C, Cho SH, Wang L, Lee LP, Wan Y. Nat Nanotechnol 19 818-824 (2024)
  47. Form factor determination of biological molecules with X-ray free electron laser small-angle scattering (XFEL-SAS). Blanchet CE, Round A, Mertens HDT, Ayyer K, Graewert M, Awel S, Franke D, Dörner K, Bajt S, Bean R, Custódio TF, de Wijn R, Juncheng E, Henkel A, Gruzinov A, Jeffries CM, Kim Y, Kirkwood H, Kloos M, Knoška J, Koliyadu J, Letrun R, Löw C, Makroczyova J, Mall A, Meijers R, Pena Murillo GE, Oberthür D, Round E, Seuring C, Sikorski M, Vagovic P, Valerio J, Wollweber T, Zhuang Y, Schulz J, Haas H, Chapman HN, Mancuso AP, Svergun D. Commun Biol 6 1057 (2023)
  48. Isolation, characterization, and structure-based engineering of a neutralizing nanobody against SARS-CoV-2. Li T, Zhou B, Li Y, Huang S, Luo Z, Zhou Y, Lai Y, Gautam A, Bourgeau S, Wang S, Bao J, Tan J, Lavillette D, Li D. Int J Biol Macromol 209 1379-1388 (2022)
  49. Simple Affinity-Based Method for Concentrating Viruses from Wastewater Using Engineered Curli Fibers. Birnbaum DP, Vilardi KJ, Anderson CL, Pinto AJ, Joshi NS. ACS ES T Water 2 1836-1843 (2022)
  50. Structural and functional characterization of nanobodies that neutralize Omicron variants of SARS-CoV-2. Cornish K, Huo J, Jones L, Sharma P, Thrush JW, Abdelkarim S, Kipar A, Ramadurai S, Weckener M, Mikolajek H, Liu S, Buckle I, Bentley E, Kirby A, Han X, Laidlaw SM, Hill M, Eyssen L, Norman C, Le Bas A, Clarke J, James W, Stewart JP, Carroll M, Naismith JH, Owens RJ. Open Biol 14 230252 (2024)
  51. A General Method to Screen Nanobodies for Cytochrome P450 Enzymes from a Yeast Surface Display Library. Sun Y, Martinez-Ramos C, Chen E, Osawa Y, Zhang H. Biomedicines 12 1863 (2024)
  52. Efficient virus detection utilizing chitin-immobilized nanobodies synthesized in Ustilago maydis. Philipp M, Müller L, Andrée M, Hussnaetter KP, Schaal H, Feldbrügge M, Schipper K. J Biotechnol 366 72-84 (2023)
  53. Multi-compartmental diversification of neutralizing antibody lineages dissected in SARS-CoV-2 spike-immunized macaques. Mandolesi M, Das H, de Vries L, Yang Y, Kim C, Dhinakaran M, Castro Dopico X, Fischbach J, Kim S, Guryleva MV, Àdori M, Chernyshev M, Stålmarck A, Hanke L, McInerney GM, Sheward DJ, Corcoran M, Hällberg BM, Murrell B, Karlsson Hedestam GB. Nat Commun 15 6338 (2024)
  54. Polyvalent Nanobody Structure Designed for Boosting SARS-CoV-2 Inhibition. Song T, Cooper L, Galván Achi J, Wang X, Dwivedy A, Rong L, Wang X. J Am Chem Soc 146 5894-5900 (2024)


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