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TitleDEVELOPMENT OF A POTENT MONOCLONAL ANTIBODY FOR TREATMENT OF HUMAN METAPNEUMOVIRUS INFECTIONS.
Journal, issue, pagesbioRxiv, Year 2025
Publish dateJul 20, 2025
AuthorsEvelyn D Harris / Morgan McGovern / Sara Pernikoff / Ren Ikeda / Lea Kipnis / William Hannon / Elizabeth B Sobolik / Matthew Gray / Alexander L Greninger / Sijia He / Chen-Ni Chin / Tong-Ming Fu / Marie Pancera / Jim Boonyaratanakornkit /
PubMed AbstractHuman metapneumovirus (HMPV) is a major cause of respiratory infections, particularly among vulnerable populations, yet effective therapeutics remain unavailable. Monoclonal antibodies (mAbs) offer a ...Human metapneumovirus (HMPV) is a major cause of respiratory infections, particularly among vulnerable populations, yet effective therapeutics remain unavailable. Monoclonal antibodies (mAbs) offer a promising approach for both treatment and prevention. Here, we describe the discovery and characterization of 4F11, a highly potent and broadly neutralizing mAb with demonstrated in vitro and in vivo efficacy against HMPV. Using cryo-electron microscopy, we defined a unique mechanism of binding HMPV employed by 4F11, which distinguishes it from previously characterized RSV and HMPV mAbs. 4F11 targets an epitope located at the apex of the prefusion F protein (site Ø) with a 1:1 stoichiometry, distinct from the 3:1 stoichiometry observed with other HMPV site Ø antibodies. Unlike other site Ø antibodies, which penetrate the glycan shield between Asn57 and Asn172, 4F11 binds vertically and directly interacts with the Asn172 glycan, representing a unique glycan-dependent mode of recognition. In vitro, 4F11 displayed high potency and broad neutralization across diverse HMPV strains. It also showed a low propensity for resistance development, with only a single escape mutation (K179E) identified, a mutation not found in any published HMPV sequence to date. Viruses rescued with the K179E escape mutation had significantly decreased fitness in vitro compared to wild-type virus. In a hamster challenge model, 4F11 significantly reduced viral loads in both the lungs and nasal turbinates. These findings highlight 4F11 as a promising candidate for therapeutic development, particularly for immunocompromised individuals and other high-risk groups.
External linksbioRxiv / PubMed:40666860 / PubMed Central
MethodsEM (single particle)
Resolution4.03 - 4.13 Å
Structure data

70773

9ore

EMDB-70773, PDB-9ore:
CryoEM structure of 4F11 Fab bound to stabilized MPV-2c HMPV preF
Method: EM (single particle) / Resolution: 4.13 Å

EMDB-70774: CryoEM map of 4F11 and MxR Fabs bound to HMPV DS-CavEs2 preF monomer
Method: EM (single particle) / Resolution: 4.03 Å

Chemicals

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

Source
  • human metapneumovirus
  • homo sapiens (human)
KeywordsIMMUNE SYSTEM / HMPV / prefusion F / ANTIBODY / site 0 / glycan dependent

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