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TitlePotent neutralization by a RBD antibody with broad specificity for SARS-CoV-2 JN.1 and other variants.
Journal, issue, pagesNpj Viruses, Vol. 2, Issue 1, Page 55, Year 2024
Publish dateNov 14, 2024
AuthorsMichael S Piepenbrink / Ahmed Magdy Khalil / Ana Chang / Ahmed Mostafa / Madhubanti Basu / Sanghita Sarkar / Simran Panjwani / Yaelyn H Ha / Yao Ma / Chengjin Ye / Qian Wang / Todd J Green / James L Kizziah / Nathaniel B Erdmann / Paul A Goepfert / Lihong Liu / David D Ho / Luis Martinez-Sobrido / Mark R Walter / James J Kobie /
PubMed AbstractSARS-CoV-2 continues to be a public health burden, driven in-part by its continued antigenic diversification and resulting emergence of new variants. By increasing herd immunity, current vaccines ...SARS-CoV-2 continues to be a public health burden, driven in-part by its continued antigenic diversification and resulting emergence of new variants. By increasing herd immunity, current vaccines have improved infection outcomes for many. However, prophylactic and treatment interventions that are not compromised by viral evolution of the Spike protein are still needed. Using a differential staining strategy with a rationally designed SARS-CoV-2 Receptor Binding Domain (RBD) - ACE2 fusion protein and a native Omicron RBD protein, we developed a recombinant human monoclonal antibody (hmAb) from a convalescent individual following SARS-CoV-2 Omicron infection. The resulting hmAb, 1301B7 potently neutralized a wide range of SARS-CoV-2 variants including the original Wuhan-1, the more recent Omicron JN.1 strain, and SARS-CoV. 1301B7 contacts the ACE2 binding site of RBD exclusively through its VH1-69 heavy chain. Broad specificity is achieved through 1301B7 binding to many conserved residues of Omicron variants including Y501 and H505. Consistent with its extensive binding epitope, 1301B7 is able to potently diminish viral burden in the upper and lower respiratory tract and protect mice from challenge with Omicron XBB1.5 and Omicron JN.1 viruses. These results suggest 1301B7 has broad potential to prevent or treat clinical SARS-CoV-2 infections and to guide development of RBD-based universal SARS-CoV-2 prophylactic vaccines and therapeutic approaches.
External linksNpj Viruses / PubMed:39553825 / PubMed Central
MethodsEM (single particle)
Resolution4.1 Å
Structure data

44666

9bll

EMDB-44666, PDB-9bll:
Cryo-EM of RBD(EG5.1)/1301B7 Fab Complex
Method: EM (single particle) / Resolution: 4.1 Å

Chemicals

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

Source
  • homo sapiens (human)
  • severe acute respiratory syndrome coronavirus 2
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / Fab / RBD / Complex / PROTEIN BINDING / VIRAL PROTEIN-IMMUNE SYSTEM complex

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