ArticleCell reports. Medicine2026
A potently neutralizing and protective human antibody targeting antigenic site V on RSV and hMPV fusion glycoprotein.
Article in Cell reports. Medicine, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed.
- Structural and functional characterization of a conserved cryptic epitope on SARS-CoV-2 spike S2 subunit.PLoS pathogens · 2026Article
- Intelligent antigen design combined with yeast display enhances targeted immune responses.Briefings in bioinformatics · 2026Article
- Article
- hMPV Outbreaks: Worldwide Implications of a Re-Emerging Respiratory Pathogen.Microorganisms · 2025Review
- Addressing SARS-CoV-2 evolution: neutralization of emerging variants of concern by the AVX/COVID-12 'Patria' vaccine based on HexaPro-S ancestral Wuhan spike or its updated BA.2.75.2 version.Frontiers in immunology · 2025Article
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18 authors.
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Abstract
Human respiratory syncytial virus (RSV) and human metapneumovirus (hMPV) are frequent drivers of morbidity and mortality in susceptible populations. The primary target of neutralizing antibodies is the fusion (F) glycoprotein on the surface of the RSV and hMPV virion. As a result of the structural conservation between RSV and hMPV F, three antigenic regions are known to induce cross-neutralizing responses: sites III, IV, and V. Leveraging LIBRA-seq, we identify five RSV/hMPV cross-reactive human antibodies. One antibody, RM 5-1, potently neutralizes all tested viruses from the major subgroups of RSV and hMPV and provides protection against RSV and hMPV in a mouse challenge model. Structural analysis reveals that RM 5-1 utilizes an uncommon genetic signature to bind an epitope that spans sites Ø, II, and V. These findings highlight the molecular and structural elements influencing RSV and hMPV cross-reactivity as well as the potential of antibody RM 5-1 for translational development.
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