Evidence map›Paper›PMID 29142300›Full record

ArticleNature communications2017

Structure and immunogenicity of pre-fusion-stabilized human metapneumovirus F glycoprotein.

Michael B Battles, Vicente Más, Eduardo Olmedillas, Olga Cano, Mónica Vázquez, Laura Rodríguez, José A Melero, Jason S McLellan

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
5.3field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

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.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

96 citing papers in PubMed, 120 citations in OpenAlex.

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  12. Molecular Evolution of theMicroorganisms · 2026
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36 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 2 institutions in 2 countries.

Michael B BattlesDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, NH, 03755, USA.ORCID http://orcid.org/0000-0002-5321-7460
Vicente MásUnidad de Biología Viral, Centro Nacional de Microbiología and CIBER de Enfermedades Respiratorias, Instituto de Salud Carlos III, 28220, Madrid, Spain.
Eduardo OlmedillasUnidad de Biología Viral, Centro Nacional de Microbiología and CIBER de Enfermedades Respiratorias, Instituto de Salud Carlos III, 28220, Madrid, Spain.
Olga CanoUnidad de Biología Viral, Centro Nacional de Microbiología and CIBER de Enfermedades Respiratorias, Instituto de Salud Carlos III, 28220, Madrid, Spain.
Mónica VázquezUnidad de Biología Viral, Centro Nacional de Microbiología and CIBER de Enfermedades Respiratorias, Instituto de Salud Carlos III, 28220, Madrid, Spain.
Laura RodríguezUnidad de Biología Viral, Centro Nacional de Microbiología and CIBER de Enfermedades Respiratorias, Instituto de Salud Carlos III, 28220, Madrid, Spain.
José A MeleroUnidad de Biología Viral, Centro Nacional de Microbiología and CIBER de Enfermedades Respiratorias, Instituto de Salud Carlos III, 28220, Madrid, Spain. jmelero@isciii.es.
Jason S McLellanDepartment of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, NH, 03755, USA. Jason.S.McLellan@Dartmouth.edu.
Instituto de Salud Carlos III · ESDartmouth College · US

Funding

Understanding the role of RNA-binding protein mutations in cancerP20GM113132 · NIGMS · DARTMOUTH COLLEGE · PI MADDEN, DEAN R · 2016 to 2025
$25.9M
HOST-MICROBE INTERACTIONST32AI007519 · NIAID · DARTMOUTH COLLEGE · PI DEBORAH A HOGAN · 1997 to 2026
$5.9M
NIAID NIH HHS T32 AI007519NIGMS NIH HHS P20 GM113132
6 · The paper itself

Abstract

Human metapneumovirus (hMPV) is a frequent cause of bronchiolitis in young children. Its F glycoprotein mediates virus-cell membrane fusion and is the primary target of neutralizing antibodies. The inability to produce recombinant hMPV F glycoprotein in the metastable pre-fusion conformation has hindered structural and immunological studies. Here, we engineer a pre-fusion-stabilized hMPV F ectodomain and determine its crystal structure to 2.6 Å resolution. This structure reveals molecular determinants of strain-dependent acid-induced fusion, as well as insights into refolding from pre- to post-fusion conformations. A dense glycan shield at the apex of pre-fusion hMPV F suggests that antibodies against this site may not be elicited by host immune responses, which is confirmed by depletion studies of human immunoglobulins and by mouse immunizations. This is a major difference with pre-fusion F from human respiratory syncytial virus (hRSV), and collectively our results should facilitate development of effective hMPV vaccine candidates.

Indexed as

AnimalsAntibodies, NeutralizingAntibodies, ViralChlorocebus aethiopsCrystallography, X-RayFemaleImmunoglobulins, IntravenousMetapneumovirusMiceMice, Inbred BALB CProtein DomainsProtein EngineeringProtein RefoldingRecombinant ProteinsRespiratory Syncytial Virus, HumanVero CellsAntibodies, NeutralizingAntibodies, ViralImmunoglobulins, IntravenousRecombinant ProteinsViral Fusion Proteins

Identifiers

PMID29142300
PMCPMC5688127
OpenAlexW2767506818

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

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 OpenQuestion graph.