ArticlePLoS pathogens2016
Engineering, Structure and Immunogenicity of the Human Metapneumovirus F Protein in the Postfusion Conformation.
Article in PLoS pathogens, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers, 1 of them a synthesis that pooled it.
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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.
The trial behind it
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
52 citing papers in PubMed, 1 synthesis or guideline pooled it, 76 citations in OpenAlex.
- Insights into the multifunctionality of viral glycoproteins F and HN in the lifecycle and pathogenesis of Newcastle disease virus: a systematic review.Veterinary research · 2025Pooled it
- Distinct mechanisms of neutralization by antibodies targeting a conserved pneumovirus F epitope.bioRxiv : the preprint server for biology · 2026Article
- Twenty-five years of human metapneumovirus research.Clinical microbiology reviews · 2026Review
- Stabilization of prefusion hMPV F improves manufacturability and protective immunity across hMPV lineages.Virologica Sinica · 2026Article
- A novel antiviral strategy targeting human metapneumovirus through pH modulation in human airway epithelial cells.The Journal of general virology · 2026Article
- Global distribution and evolution of human metapneumovirus A2b2 clade: Insights from genomic surveillance.Epidemiology and infection · 2026Article
- Machine learning and molecular modeling reveal potential inhibitors of the human metapneumovirus fusion protein.Molecular diversity · 2026Article
- Emergence and Molecular Epidemiology of Human Metapneumovirus in Greece in the Post-COVID Era.International journal of molecular sciences · 2026Article
- Mechanistic insights and emerging applications of human metapneumovirus (HMPV) treatment: From molecular design to translational immunity.Folia microbiologica · 2026Review
- Avian Metapneumovirus: Virology, Epidemiology, and Insights from a Comparative Analysis with Human Metapneumovirus-A Review.Biomolecules · 2026Review
- A potently neutralizing and protective human antibody targeting antigenic site V on RSV and hMPV fusion glycoprotein.Cell reports. Medicine · 2026Article
- Molecular Evolution of theMicroorganisms · 2026Article
- Article
- Genetic and epidemiological characteristics of the spread of human metapneumovirus in Bulgaria, 2023-2025.Frontiers in public health · 2026Article
- In silico prediction, molecular docking and simulation of natural flavonoid apigenin and xanthoangelol E against human metapneumovirus.In silico pharmacology · 2026Article
- Structural basis for childhood antibody recognition of the human metapneumovirus fusion protein.Nature communications · 2025Article
- Repurposing SARS CoV 2 ligands identifies salvianolic acid C as potential antiviral candidate against human metapneumovirus through computational study.Scientific reports · 2025Article
- Structural Basis for Childhood Antibody Recognition of The Human Metapneumovirus Fusion Protein.bioRxiv : the preprint server for biology · 2025Article
- Using COVID-19 pandemic perturbation to model RSV-hMPV interactions and potential implications under RSV interventions.Nature communications · 2025Article
- Review: Knowledge Gained and Gaps in Understanding in the 25 Years Since Human Metapneumovirus Was First Identified as a Cause of Human Disease.The Journal of infectious diseases · 2025Review
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Human metapneumovirus (hMPV) is a paramyxovirus that is a common cause of bronchiolitis and pneumonia in children less than five years of age. The hMPV fusion (F) glycoprotein is the primary target of neutralizing antibodies and is thus a critical vaccine antigen. To facilitate structure-based vaccine design, we stabilized the ectodomain of the hMPV F protein in the postfusion conformation and determined its structure to a resolution of 3.3 Å by X-ray crystallography. The structure resembles an elongated cone and is very similar to the postfusion F protein from the related human respiratory syncytial virus (hRSV). In contrast, significant differences were apparent with the postfusion F proteins from other paramyxoviruses, such as human parainfluenza type 3 (hPIV3) and Newcastle disease virus (NDV). The high similarity of hMPV and hRSV postfusion F in two antigenic sites targeted by neutralizing antibodies prompted us to test for antibody cross-reactivity. The widely used monoclonal antibody 101F, which binds to antigenic site IV of hRSV F, was found to cross-react with hMPV postfusion F and neutralize both hRSV and hMPV. Despite the cross-reactivity of 101F and the reported cross-reactivity of two other antibodies, 54G10 and MPE8, we found no detectable cross-reactivity in the polyclonal antibody responses raised in mice against the postfusion forms of either hMPV or hRSV F. The postfusion-stabilized hMPV F protein did, however, elicit high titers of hMPV-neutralizing activity, suggesting that it could serve as an effective subunit vaccine. Structural insights from these studies should be useful for designing novel immunogens able to induce wider cross-reactive antibody responses.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.