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TitleAntibody cocktails based on the occupationally acquired immunity of pediatricians neutralize and confer protection against RSV and hMPV.
Journal, issue, pagesSci Transl Med, Vol. 18, Issue 837, Page eadz4170, Year 2026
Publish dateFeb 18, 2026
AuthorsHui Zhai / Wenxiang Yu / Jinyue Wang / Jie Deng / Siyu Lei / Teng Zhou / Yixin Li / Kaijun Xu / Mengyang Ma / Rui Feng / Yaling Hu / Luo Ren / Yunlong Cao / Enmei Liu / Xiangxi Wang /
PubMed AbstractHuman respiratory syncytial virus (RSV) and human metapneumovirus (hMPV) are major causes of severe respiratory infections in young children, older adults, and immunocompromised individuals. Here, we ...Human respiratory syncytial virus (RSV) and human metapneumovirus (hMPV) are major causes of severe respiratory infections in young children, older adults, and immunocompromised individuals. Here, we isolated RSV fusion (F) protein-specific B cells from pediatricians who are routinely exposed to these viruses. We then derived monoclonal antibodies (mAbs) from those B cells to characterize their binding and neutralization profiles. Among the isolated mAbs, we found that CNR2056 and CNR2053 (targeting site Ø of the pre-F protein) potently neutralized diverse RSV A and B strains; another mAb, CNR2047 (targeting site III), uniquely exhibited cross-neutralization capacity against both RSV and hMPV variants. In vivo, prophylactic administration of CNR2056 and CNR2053 controlled lung viral loads and pathology in RSV A2- and B9320-challenged cotton rats. Moreover, a prophylactic dose of 0.5 milligrams per kilogram of CNR2047 resulted in complete protection against hMPV in the lungs of BALB/c mice. Structural analysis revealed unique binding modes for the three mAbs, supporting the potential for rational mAb cocktail design. Deep mutational scanning for RSV F further demonstrated that mutations required to evade CNR2053 and CNR2056 were primarily in evolutionarily constrained sites, suggesting a fitness cost to immune escape. Rationally combining site Ø- and site III-directed mAbs (e.g., CNR2056-CNR2047) into cocktails conferred additive effects, expanding coverage to hMPV and minimizing risk of escape variants. Thus, rationally designed cocktails of CNR2056, CNR2053, and CNR2047 may offer a versatile immunoprophylactic agent against a range of pneumoviruses with potential to protect against both current and future variants.
External linksSci Transl Med / PubMed:41706868
MethodsEM (single particle)
Resolution3.75 - 4.43 Å
Structure data

64666

9v0n

EMDB-64666, PDB-9v0n:
Cryo-EM structure of RSV pre-F in complex with antibody CNR2042
Method: EM (single particle) / Resolution: 3.75 Å

64667

9v0p

EMDB-64667, PDB-9v0p:
Cryo-EM structure of RSV pre-F in complex with antibody CNR2053
Method: EM (single particle) / Resolution: 3.87 Å

64668

9v0q

EMDB-64668, PDB-9v0q:
Cryo-EM structure of RSV pre-F in complex with antibody CNR2056
Method: EM (single particle) / Resolution: 3.85 Å

64670

9v0s

EMDB-64670, PDB-9v0s:
Cryo-EM structure of RSV pre-F in complex with antibody CNR2047
Method: EM (single particle) / Resolution: 3.78 Å

64671

9v0t

EMDB-64671, PDB-9v0t:
Cryo-EM structure of hMPV pre-F in complex with antibody CNR2047
Method: EM (single particle) / Resolution: 4.12 Å

64735

9v2o

EMDB-64735, PDB-9v2o:
Cryo-EM structure of RSV pre-F monomer in complex with CNR2056/CNR2047
Method: EM (single particle) / Resolution: 4.27 Å

64737

9v2q

EMDB-64737, PDB-9v2q:
Cryo-EM structure of RSV pre-F dimer in complex with CNR2056/CNR2047
Method: EM (single particle) / Resolution: 4.43 Å

64738

9v2r

EMDB-64738, PDB-9v2r:
Cryo-EM structure of RSV pre-F trimer in complex with CNR2056/CNR2047
Method: EM (single particle) / Resolution: 4.4 Å

Source
  • respiratory syncytial virus a2
  • homo sapiens (human)
  • human metapneumovirus a
KeywordsVIRAL PROTEIN / RSV / Fusion Protein / Antibody / hMPV

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