Evidence map›Paper›PMID 32923643›Full record

ArticleScience advances2020

Global and local envelope protein dynamics of hepatitis C virus determine broad antibody sensitivity.

Elias H Augestad, Matteo Castelli, Nicola Clementi, Luisa J Ströh, Thomas Krey, Roberto Burioni, Nicasio Mancini, Jens Bukh, Jannick Prentoe

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.4field-weighted citation impact, top 6% 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

27 citing papers in PubMed, 38 citations in OpenAlex.

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  7. Bispecific antibodies against the hepatitis C virus E1E2 envelope glycoprotein.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

9 authors at 3 institutions in 3 countries.

Elias H AugestadCopenhagen Hepatitis C Program (CO-HEP), Department of Infectious Diseases, Hvidovre Hospital, and Department of Immunology and Microbiology, Faculty of Health and Medical Sciences, University of Copenhagen, DK-2200 Copenhagen, Denmark.ORCID 0000-0003-0917-3971
Matteo CastelliLaboratory of Microbiology and Virology, Università "Vita-Salute" San Raffaele, Milano, 20132, Italy.
Nicola ClementiLaboratory of Microbiology and Virology, Università "Vita-Salute" San Raffaele, Milano, 20132, Italy.ORCID 0000-0002-1822-9861
Luisa J StröhInstitute of Virology, Hannover Medical School, Carl-Neuberg-Str. 1, Hannover 30625, Germany.ORCID 0000-0002-2781-2303
Thomas KreyInstitute of Virology, Hannover Medical School, Carl-Neuberg-Str. 1, Hannover 30625, Germany.ORCID 0000-0002-4548-7241
Roberto BurioniLaboratory of Microbiology and Virology, Università "Vita-Salute" San Raffaele, Milano, 20132, Italy.
Nicasio ManciniLaboratory of Microbiology and Virology, Università "Vita-Salute" San Raffaele, Milano, 20132, Italy.ORCID 0000-0003-0637-0910
Jens BukhCopenhagen Hepatitis C Program (CO-HEP), Department of Infectious Diseases, Hvidovre Hospital, and Department of Immunology and Microbiology, Faculty of Health and Medical Sciences, University of Copenhagen, DK-2200 Copenhagen, Denmark.ORCID 0000-0002-7815-4806
Jannick PrentoeCopenhagen Hepatitis C Program (CO-HEP), Department of Infectious Diseases, Hvidovre Hospital, and Department of Immunology and Microbiology, Faculty of Health and Medical Sciences, University of Copenhagen, DK-2200 Copenhagen, Denmark.ORCID 0000-0003-2203-9478
Vita-Salute San Raffaele University · ITHvidovre Hospital · DKMedizinische Hochschule Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Broad antibody sensitivity differences of hepatitis C virus (HCV) isolates and their ability to persist in the presence of neutralizing antibodies (NAbs) remain poorly understood. Here, we show that polymorphisms within glycoprotein E2, including hypervariable region 1 (HVR1) and antigenic site 412 (AS412), broadly affect NAb sensitivity by shifting global envelope protein conformation dynamics between theoretical "closed," neutralization-resistant and "open," neutralization-sensitive states. The conformational space of AS412 was skewed toward β-hairpin-like conformations in closed states, which also depended on HVR1, assigning function to these enigmatic E2 regions. Scavenger receptor class B, type I entry dependency of HCV was associated with NAb resistance and correlated perfectly with decreased virus propensity to interact with HCV co-receptor CD81, indicating that decreased NAb sensitivity resulted in a more complex entry pathway. This link between global E1/E2 states and functionally distinct AS412 conformations has important implications for targeting AS412 in rational HCV vaccine designs.

Indexed as

HepacivirusHepatitis CAntibodies, NeutralizingHepatitis C AntibodiesHumansViral Envelope ProteinsAntibodies, NeutralizingHepatitis C AntibodiesViral Envelope Proteins

Identifiers

PMID32923643
PMCPMC7449684
OpenAlexW3080286256

What OpenQuestion holds

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LicenceCC BY-NC
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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.