Evidence map›Paper›PMID 28799905›Full record

ReviewCell host & microbe2017

Principles of Broad and Potent Antiviral Human Antibodies: Insights for Vaccine Design.

James E Crowe

Open access · bronzeAbstract readReview
In one paragraph

Review in Cell host & microbe, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

47 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Antibodies: what makes us stronger.Human vaccines & immunotherapeutics · 2021
    Article
  15. Article
  16. Article
  17. Article
  18. Subdominance in Antibody Responses: Implications for Vaccine Development.Microbiology and molecular biology reviews : MMBR · 2020
    Review
  19. Article
  20. Article
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

1 author at 1 institution in 1 country.

James E CroweVanderbilt Vaccine Center, Vanderbilt University Medical Center, Nashville, TN 37232, USA; Department of Pathology, Microbiology and Immunology, Vanderbilt University, Nashville, TN 37232, USA; Department of Pediatrics, Vanderbilt University School of Medicine, Nashville, TN 37232, USA. Electronic address: james.crowe@vanderbilt.edu.
Vanderbilt University Medical Center · US

Funding

Supplemental Research Project (SRP)U19AI109711 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI GEISBERT, THOMAS WILLIAM · 2014 to 2018
$26.6M
Structure based design of antibodies and vaccinesU19AI117905 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI SCHIEF, WILLIAM R. · 2015 to 2019
$12.0M
Human neutralizing antibodies for Zika virusR01AI127828 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI CROWE, JAMES E, DIAMOND, MICHAEL S · 2017 to 2021
$3.9M
Structural and functional basis of ultra potent CHKV neutralization by human mAbsR01AI114816 · NIAID · VANDERBILT UNIVERSITY MEDICAL CENTER · PI CROWE, JAMES E, DIAMOND, MICHAEL S · 2015 to 2019
$3.7M
NIAID NIH HHS HHSN272201400024CNIAID NIH HHS R01 AI114816NIAID NIH HHS R01 AI127828NIAID NIH HHS U19 AI109711NIAID NIH HHS U19 AI117905
6 · The paper itself

Abstract

Antibodies are the principal immune effectors that mediate protection against reinfection following viral infection or vaccination. Robust techniques for human mAb isolation have been developed in the last decade. The study of human mAbs isolated from subjects with prior immunity has become a mainstay for rational structure-based, next-generation vaccine development. The plethora of detailed molecular and genetic studies coupling the structure of antigen-antibody complexes with their antiviral function has begun to reveal common principles of critical interactions on which we can build better vaccines and therapeutic antibodies. This review outlines the approaches to isolating and studying human antiviral mAbs and discusses the common principles underlying the basis for their activity. This review also examines progress toward the goal of achieving a comprehensive understanding of the chemical and physical basis for molecular recognition of viral surface proteins in order to build predictive molecular models that can be used for vaccine design.

Indexed as

Antiviral AgentsDrug DesignAnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralAntigens, ViralCross ReactionsGenes, ReporterHumansImmunityModels, MolecularNeutralization TestsProtein Structure, QuaternaryVaccinationVaccinesAntibodies, MonoclonalAntibodies, NeutralizingAntibodies, ViralAntigens, ViralAntiviral AgentsVaccinesViral Envelope Proteinsantibodiesdengue virusEbola virushumaninfluenza virusMarburg virusmonoclonal antibodiesneutralization

Identifiers

PMID28799905
PMCPMC5700460
OpenAlexW2743687550

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.