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TitleDeciphering a reliable synergistic bispecific strategy of rescuing antibodies for SARS-CoV-2 escape variants, including BA.2.86, EG.5.1, and JN.1.
Journal, issue, pagesCell Rep, Vol. 43, Issue 6, Page 114338, Year 2024
Publish dateJun 25, 2024
AuthorsZhou Tong / Jianyu Tong / Wenwen Lei / Yufeng Xie / Yingzi Cui / Guowen Jia / Shihua Li / Zezhong Zhang / Zhimin Cheng / Xiao Xing / Haiyun Ma / Lan Deng / Rong Zhang / Xin Zhao / Kefang Liu / Qihui Wang / Jianxun Qi / Haomin Huang / Rui Song / Zhaoming Su / Guizhen Wu / Jing Lou / George Fu Gao /
PubMed AbstractThe game between therapeutic monoclonal antibodies (mAbs) and continuously emerging severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants has favored the virus, as most therapeutic ...The game between therapeutic monoclonal antibodies (mAbs) and continuously emerging severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) variants has favored the virus, as most therapeutic mAbs have been evaded. Addressing this challenge, we systematically explored a reproducible bispecific antibody (bsAb)-dependent synergistic effect in this study. It could effectively restore the neutralizing activity of the bsAb when any of its single mAbs is escaped by variants. This synergy is primarily attributed to the binding angle of receptor-binding domain (RBD)-5, facilitating inter-spike cross-linking and promoting cryptic epitope exposure that classical antibody cocktails cannot achieve. Furthermore, RBD-5 with RBD-2, RBD-6, and RBD-7, alongside RBD-8, also exhibit significantly enhanced effects. This study not only shifts the paradigm in understanding antibody interactions but paves the way for developing more effective therapeutic antibodies against rapidly mutating SARS-CoV-2, with Dia-19 already showing promise against emerging variants like BA.2.86, EG.5.1, and JN.1.
External linksCell Rep / PubMed:38850530
MethodsEM (single particle)
Resolution2.1 - 3.2 Å
Structure data

38617

8xse

EMDB-38617, PDB-8xse:
SARS-CoV-2 RBD + IMCAS-123 + IMCAS-72 Fab
Method: EM (single particle) / Resolution: 2.5 Å

38618

8xsf

EMDB-38618, PDB-8xsf:
SARS-CoV-2 RBD + IMCAS-364 + hACE2
Method: EM (single particle) / Resolution: 2.16 Å

38619

8xsi

EMDB-38619, PDB-8xsi:
SARS-CoV-2 RBD + IMCAS-364 (Local Refinement)
Method: EM (single particle) / Resolution: 2.1 Å

38620

8xsj

EMDB-38620, PDB-8xsj:
SARS-CoV-2 Omicron BA.4 RBD + IMCAS-316 + ACE2
Method: EM (single particle) / Resolution: 2.61 Å

38621

8xsl

EMDB-38621, PDB-8xsl:
SARS-CoV-2 spike + IMCAS-123
Method: EM (single particle) / Resolution: 3.2 Å

38823

8y0y

EMDB-38823, PDB-8y0y:
Cryo-EM structure of the 123-316 scDb/PT-RBD complex
Method: EM (single particle) / Resolution: 2.86 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-ZN:
Unknown entry

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / SARS-CoV-2 / broadly neutralizing antibodies / VIRUS / VIRAL PROTEIN-IMMUNE SYSTEM complex / VIRAL PROTEIN/HYDROLASE/IMMUNE SYSTEM / VIRAL PROTEIN-HYDROLASE-IMMUNE SYSTEM complex / ANTIVIRAL PROTEIN / VIRAL PROTEIN-ANTIVIRAL PROTEIN complex / IMMUNE SYSTEM / Cryo-EM / SARS-CoV2 / antibody / RBD

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