Evidence map›Paper›PMID 36702826›Full record

ArticleNature communications2023

Regions of hepatitis C virus E2 required for membrane association.

Ashish Kumar, Tiana C Rohe, Elizabeth J Elrod, Abdul G Khan, Altaira D Dearborn, Ryan Kissinger, Arash Grakoui, Joseph Marcotrigiano

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
3.7field-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

11 citing papers in PubMed, 18 citations in OpenAlex.

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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

8 authors at 3 institutions in 1 country.

Ashish Kumar *Structural Virology Section, Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, 20892, USA.
Tiana C Rohe *Structural Virology Section, Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, 20892, USA.
Elizabeth J ElrodEmory National Primate Research Center, Division of Microbiology and Immunology, Emory Vaccine Center, Emory University School of Medicine, Atlanta, GA, 30329, USA.
Abdul G KhanCenter for Advanced Biotechnology and Medicine, Rutgers, The State University of New Jersey, Piscataway, NJ, 08854, USA.
Altaira D DearbornStructural Virology Section, Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, 20892, USA.
Ryan KissingerResearch Technology Branch, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT, 59840, USA.ORCID 0000-0002-3628-9710
Arash GrakouiEmory National Primate Research Center, Division of Microbiology and Immunology, Emory Vaccine Center, Emory University School of Medicine, Atlanta, GA, 30329, USA.ORCID 0000-0002-6002-7518
Joseph MarcotrigianoStructural Virology Section, Laboratory of Infectious Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD, 20892, USA. joseph.marcotrigiano@nih.gov.ORCID 0000-0001-7670-7836
National Institutes of Health · USEmory University · USRutgers, The State University of New Jersey · US

Funding

Protective immunity to HCV and rational vaccine designU19AI159819 · NIAID · EMORY UNIVERSITY · PI Rama Rao Amara · 2021 to 2026
$16.6M
Entry and replication of positive-sense, RNA virusesZIAAI001217 · NIAID · NATIONAL INSTITUTE OF ALLERGY AND INFECTIOUS DISEASES · PI MARCOTRIGIANO, JOSEPH · 2017 to 2025
$11.0M
Dynamics of antigen specific B and Tfh responses during acute and chronic HCVR01AI136533 · NIAID · EMORY UNIVERSITY · PI GRAKOUI, ARASH · 2018 to 2022
$3.8M
NIAID NIH HHS R01 AI136533NIAID NIH HHS U19 AI159819
6 · The paper itself

Abstract

Hepatitis C virus (HCV) uses a hybrid entry mechanism. Current structural data suggest that upon exposure to low pH and Cluster of Differentiation 81 (CD81), the amino terminus of envelope glycoprotein E2 becomes ordered and releases an internal loop with two invariant aromatic residues into the host membrane. Here, we present the structure of an amino-terminally truncated E2 with the membrane binding loop in a bent conformation and the aromatic side chains sequestered. Comparison with three previously reported E2 structures with the same Fab indicates that this internal loop is flexible, and that local context influences the exposure of hydrophobic residues. Biochemical assays show that the amino-terminally truncated E2 lacks the baseline membrane-binding capacity of the E2 ectodomain. Thus, the amino terminal region is a critical determinant for both CD81 and membrane interaction. These results provide new insights into the HCV entry mechanism.

Indexed as

HepacivirusHepatitis CHumansProtein BindingTetraspanin 28Viral Envelope ProteinsTetraspanin 28Viral Envelope Proteins

Identifiers

PMID36702826
PMCPMC9879980
OpenAlexW4318069740

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.