Evidence map›Paper›PMID 25002515›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2014

Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization.

Lu Deng, Li Ma, Maria Luisa Virata, Lilin Zhong, Hailing Yan, Zhong Zhao, Evi Struble, Stephen Feinstone, Harvey Alter, Pei Zhang

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
–field-weighted citation impact
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

31 citing papers in PubMed.

  1. Trial
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  8. HCV Glycoprotein Structure and Implications for B-Cell Vaccine Development.International journal of molecular sciences · 2020
    Review
  9. Review
  10. Article
  11. Article
  12. Disordered epitopes as peptide vaccines.Peptide science (Hoboken, N.J.) · 2018
    Review
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  14. Article
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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

10 authors.

Lu DengDivision of Hematology, Office of Blood Research and Review, Center for Biologics Evaluation and Research, US Food and Drug Administration, Bethesda, MD 20892;
Li MaDivision of Hematology, Office of Blood Research and Review, Center for Biologics Evaluation and Research, US Food and Drug Administration, Bethesda, MD 20892;
Maria Luisa VirataDivision of Hematology, Office of Blood Research and Review, Center for Biologics Evaluation and Research, US Food and Drug Administration, Bethesda, MD 20892;
Lilin ZhongDivision of Hematology, Office of Blood Research and Review, Center for Biologics Evaluation and Research, US Food and Drug Administration, Bethesda, MD 20892;
Hailing YanDivision of Hematology, Office of Blood Research and Review, Center for Biologics Evaluation and Research, US Food and Drug Administration, Bethesda, MD 20892;
Zhong ZhaoDivision of Hematology, Office of Blood Research and Review, Center for Biologics Evaluation and Research, US Food and Drug Administration, Bethesda, MD 20892;
Evi StrubleDivision of Hematology, Office of Blood Research and Review, Center for Biologics Evaluation and Research, US Food and Drug Administration, Bethesda, MD 20892;
Stephen FeinstoneDepartment of Biochemistry and Molecular Medicine, George Washington University School of Medicine and Health Sciences, Washington, DC 20037; and.
Harvey AlterDepartment of Transfusion Medicine, Warren Grant Magnuson Clinical Center, National Institutes of Health, Bethesda, MD 20892 pei.zhang@fda.hhs.gov halter@dtm.cc.nih.gov.
Pei ZhangDivision of Hematology, Office of Blood Research and Review, Center for Biologics Evaluation and Research, US Food and Drug Administration, Bethesda, MD 20892; pei.zhang@fda.hhs.gov halter@dtm.cc.nih.gov.

Funding

Life Science and Biomedical technology Research center at NSLS-II LSBRP41GM111244 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI MCSWEENEY, SEAN · 2014 to 2018
$16.4M
A Prospective Study Of Anti-hepatitis C Virus Positive Blood DonorsZIACL002068 · CLC · CLINICAL CENTER · PI DE GIORGI, VALERIA · 2009 to 2025
$0k
Viral And Immune Factors That Influence Recovery Or Progression Of Hepatitis CZIACL002078 · CLC · CLINICAL CENTER · PI DE GIORGI, VALERIA · 2009 to 2025
$0k
NIGMS NIH HHS P41 GM111244
6 · The paper itself

Abstract

The X-ray crystal structure of epitope II on the E2 protein of hepatitis C virus, in complex with nonneutralizing antibody mAb#12, has been solved at 2.90-Å resolution. The spatial arrangement of the essential components of epitope II (ie, the C-terminal α-helix and the N-terminal loop) was found to deviate significantly from that observed in those corresponding complexes with neutralizing antibodies. The distinct conformations are mediated largely by the flexibility of a highly conserved glycine residue that connects these components. Thus, it is the particular tertiary structure of epitope II, which is presented in a spatial and temporal manner, that determines the specificity of antibody recognition and, consequently, the outcome of neutralization or nonneutralization.

Indexed as

Neutralization TestsAmino Acid SequenceAntibodies, NeutralizingConserved SequenceCrystallography, X-RayEpitopesHepacivirusHepatitis C AntibodiesModels, MolecularMolecular Sequence DataProtein ConformationViral Envelope ProteinsAntibodies, NeutralizingEpitopesglycoprotein E2, Hepatitis C virusHepatitis C AntibodiesViral Envelope Proteinsimmunoglobulinsprophylaxisvaccine

Identifiers

PMID25002515
PMCPMC4115556

What OpenQuestion holds

Textmetadata
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.