Evidence map›Paper›PMID 21549714›Full record

ArticleJournal of molecular biology2011

Design and characterization of epitope-scaffold immunogens that present the motavizumab epitope from respiratory syncytial virus.

Jason S McLellan, Bruno E Correia, Man Chen, Yongping Yang, Barney S Graham, William R Schief, Peter D Kwong

Abstract read
In one paragraph

Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
5.4field-weighted citation impact, top 4% 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

75 citing papers in PubMed, 111 citations in OpenAlex.

  1. Deep learning-enabled scaffolding of spatial arrays of PfCSP epitopes.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
  3. Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Review
  9. Article
  10. Adaptation-proof SARS-CoV-2 vaccine design.Advanced functional materials · 2022
    Article
  11. Article
  12. Review
  13. Article
  14. Toward rational vaccine engineering.Advanced drug delivery reviews · 2022
    Review
  15. Review
  16. Article
  17. Vaccine development lessons between HIV and COVID-19.The Lancet. Infectious diseases · 2021
    Article
  18. Review
  19. Article
  20. Article

15 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

7 authors at 3 institutions in 2 countries.

Jason S McLellanVaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA. mclellanja@mail.nih.gov
Bruno E Correia
Man Chen
Yongping Yang
Barney S Graham
William R Schief
Peter D Kwong
National Institutes of Health · USNational Institute of Allergy and Infectious Diseases · USUniversity of Washington · US

Funding

Design Of ImmunogensZIAAI005024 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI ZHOU, TONGQING · 2009 to 2025
$21.5M
Vectors and Methods to Increase Immunogenicity during DNA VaccinationZIAAI005061 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI GRAHAM, BARNEY · 2009 to 2017
$7.7M
Intramural NIH HHS ZIA AI005061
6 · The paper itself

Abstract

Respiratory syncytial virus (RSV) is a major cause of respiratory tract infections in infants, but an effective vaccine has not yet been developed. An ideal vaccine would elicit protective antibodies while avoiding virus-specific T-cell responses, which have been implicated in vaccine-enhanced disease with previous RSV vaccines. We propose that heterologous proteins designed to present RSV-neutralizing antibody epitopes and to elicit cognate antibodies have the potential to fulfill these vaccine requirements, as they can be fashioned to be free of viral T-cell epitopes. Here we present the design and characterization of three epitope-scaffolds that present the epitope of motavizumab, a potent neutralizing antibody that binds to a helix-loop-helix motif in the RSV fusion glycoprotein. Two of the epitope-scaffolds could be purified, and one epitope-scaffold based on a Staphylococcus aureus protein A domain bound motavizumab with kinetic and thermodynamic properties consistent with the free epitope-scaffold being stabilized in a conformation that closely resembled the motavizumab-bound state. This epitope-scaffold was well folded as assessed by circular dichroism and isothermal titration calorimetry, and its crystal structure (determined in complex with motavizumab to 1.9 Å resolution) was similar to the computationally designed model, with all hydrogen-bond interactions critical for binding to motavizumab preserved. Immunization of mice with this epitope-scaffold failed to elicit neutralizing antibodies but did elicit sera with F binding activity. The elicitation of F binding antibodies suggests that some of the design criteria for eliciting protective antibodies without virus-specific T-cell responses are being met, but additional optimization of these novel immunogens is required.

Indexed as

Amino Acid SequenceAntibodies, MonoclonalAntibodies, Monoclonal, HumanizedCalorimetryCell LineCircular DichroismEpitopesHumansModels, MolecularMolecular Sequence DataRespiratory Syncytial VirusesStaphylococcal Protein AAntibodies, MonoclonalAntibodies, Monoclonal, HumanizedEpitopesmotavizumabStaphylococcal Protein A

Identifiers

PMID21549714
PMCPMC3107930
OpenAlexW2083637922

What OpenQuestion holds

Textmetadata
LicenceTDM
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.