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TitleBroad Neutralizing Activity of Monoclonal Antibodies Against the Omicron Variants Isolated From Patients With Early Severe Acute Respiratory Syndrome Coronavirus-2.
Journal, issue, pagesJ Med Virol, Vol. 98, Issue 5, Page e70969, Year 2026
Publish dateJul 16, 2026
AuthorsDa Sol Kim / Uijin Kim / Hye-Min Woo / Hansaem Lee / Eun-Seong Jo / Min Jeong Noh / So-Young Lee / Byoung Kwon Park / Jeong-Sun Yang / Kyung-Chang Kim / Joo-Yeon Lee / Dong-Min Wang / Hyun-Soo Cho / Hyun-Joo Kim /
PubMed AbstractSince its emergence in 2019, severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has caused a global pandemic driven by rapid mutation and high transmissibility. Current therapeutic ...Since its emergence in 2019, severe acute respiratory syndrome coronavirus-2 (SARS-CoV-2) has caused a global pandemic driven by rapid mutation and high transmissibility. Current therapeutic strategies may not effectively address the continuously evolving mutant strains, underscoring the need for treatments with broad neutralizing activity. Two monoclonal antibodies (mAbs): SR-23 and CS-42, isolated from convalescent patients infected with SARS-CoV-2 during the early phase of the 2020 pandemic, demonstrated significant neutralizing activities against a variety of variants. Specifically, SR-23 exhibited neutralizing activity against BA.5 and XBB1.5, whereas CS-42 showed efficacy against Delta, BA.1, and BA.2 variants. In addition, combining the two mAbs demonstrated improved neutralization activity. Cryo-electron microscopy (cryo-EM) structural analysis revealed that SR-23 and CS-42 bind to nonoverlapping epitopes on the SARS-CoV-2 spike protein. Furthermore, both antibodies exhibited strong therapeutic effects in K18-hACE2 mice infected with D614G, BA.2, and XBB.1.5. These findings provide insights into the development of antibody-based therapeutics targeting emerging Omicron variants and suggest that combined administration could broaden neutralizing activity.
External linksJ Med Virol / PubMed:42126192 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.2 Å
Structure data

66860

9xgw

EMDB-66860, PDB-9xgw:
Cryo-EM structure of SARS-CoV-2 receptor binding domain in complex with CS-42 Fab (local refinement of RBD and Fv)
Method: EM (single particle) / Resolution: 3.2 Å

66861

9xgx

EMDB-66861, PDB-9xgx:
Cryo-EM structure of SARS-CoV-2 receptor binding domain in complex with SR-23 Fab (local refinement of RBD and Fv)
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

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

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / Viral protein / antibody / VIRAL PROTEIN-IMMUNE SYSTEM complex

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