Evidence map›Paper›PMID 26588073›Full record

ArticlePLoS pathogens2015

The N-terminal Helical Region of the Hepatitis C Virus p7 Ion Channel Protein Is Critical for Infectious Virus Production.

Margaret A Scull, William M Schneider, Brenna R Flatley, Robert Hayden, Canny Fung, Christopher T Jones, Marieke van de Belt, François Penin, Charles M Rice

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.6field-weighted citation impact, top 16% 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

15 citing papers in PubMed, 19 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

9 authors at 2 institutions in 2 countries.

Margaret A ScullCenter for the Study of Hepatitis C, The Rockefeller University, New York, New York, United States of America.
William M SchneiderCenter for the Study of Hepatitis C, The Rockefeller University, New York, New York, United States of America.
Brenna R FlatleyCenter for the Study of Hepatitis C, The Rockefeller University, New York, New York, United States of America.
Robert HaydenCenter for the Study of Hepatitis C, The Rockefeller University, New York, New York, United States of America.
Canny FungCenter for the Study of Hepatitis C, The Rockefeller University, New York, New York, United States of America.
Christopher T JonesCenter for the Study of Hepatitis C, The Rockefeller University, New York, New York, United States of America.
Marieke van de BeltCenter for the Study of Hepatitis C, The Rockefeller University, New York, New York, United States of America.
François PeninBases Moléculaires et Structurales des Systèmes Infectieux, IBCP, Labex Ecofect, Université Lyon 1, France; CNRS, UMR 5086, Lyon, France.
Charles M RiceCenter for the Study of Hepatitis C, The Rockefeller University, New York, New York, United States of America.
Rockefeller University · USUniversité Claude Bernard Lyon 1 · FR

Funding

Role of HCV p7 and NS2 in infectious virus productionR01AI075099 · NIAID · ROCKEFELLER UNIVERSITY · PI RICE, CHARLES M · 2008 to 2012
$2.1M
Characterization of the HCV p7 ProteinF32DK081193 · NIDDK · ROCKEFELLER UNIVERSITY · PI JONES, CHRISTOPHER T · 2007 to 2009
$159k
Characterization and Consequences of HCV Interaction with Host LipoproteinsF32AI091207 · NIAID · ROCKEFELLER UNIVERSITY · PI SCULL, MARGARET ADELE · 2010 to 2012
$146k
NIAID NIH HHS F32 AI091207NIAID NIH HHS R01 AI075099NIDDK NIH HHS F32 DK081193NIDDK NIH HHS F32DK081193
6 · The paper itself

Abstract

The hepatitis C virus (HCV) p7 protein is required for infectious virus production via its role in assembly and ion channel activity. Although NMR structures of p7 have been reported, the location of secondary structural elements and orientation of the p7 transmembrane domains differ among models. Furthermore, the p7 structure-function relationship remains unclear. Here, extensive mutagenesis, coupled with infectious virus production phenotyping and molecular modeling, demonstrates that the N-terminal helical region plays a previously underappreciated yet critical functional role, especially with respect to E2/p7 cleavage efficiency. Interrogation of specific N-terminal helix residues identified as having p7-specific defects and predicted to point toward the channel pore, in a context of independent E2/p7 cleavage, further supports p7 as a structurally plastic, minimalist ion channel. Together, our findings indicate that the p7 N-terminal helical region is critical for E2/p7 processing, protein-protein interactions, ion channel activity, and infectious HCV production.

Indexed as

Amino Acid SequenceCell LineHepacivirusHumansIon ChannelsModels, MolecularViral Envelope ProteinsViral ProteinsViroporin ProteinsVirus AssemblyVirus ReplicationIon Channelsp7 protein, Hepatitis C virusViral Envelope ProteinsViral ProteinsViroporin Proteins

Identifiers

PMID26588073
PMCPMC4654572
OpenAlexW2178413120

What OpenQuestion holds

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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.