ArticleCell reports2022
Sites of vulnerability in HCV E1E2 identified by comprehensive functional screening.
Article in Cell reports, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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.
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.
Who cites it
19 citing papers in PubMed, 29 citations in OpenAlex.
- Structure-based design of stable recombinant hepatitis C virus E1E2 heterodimers.Nature communications · 2026Article
- mAbClust with AlphaFold 3 avoids hallucinations to define a quaternary broadly neutralizing HCV epitope.bioRxiv : the preprint server for biology · 2026Article
- Antibody responses to a highly conserved peptide in HCV E2 protein correlate with chronicity or spontaneous clearance of HCV infection.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Hepatitis C virus E1 protein-specific linear B-cell epitopes, pan-genotype reactivity, and functional relevance.Frontiers in immunology · 2026Article
- Interplay of host and viral genetic variations in modulating antibody responses to genotype 3a hepatitis C virus: Implications for vaccine design.Cell reports · 2025Article
- Selection and characterization of a broadly neutralizing class of HCV anti-E2 VH1-69 antibodies.PLoS pathogens · 2025Article
- Non-cognate ligands of hepatitis C virus envelope broadly neutralizing antibodies induce virus-neutralizing sera in mice.Frontiers in immunology · 2025Article
- Article
- The red algaProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Hepatitis C Virus E1E2 Structure, Diversity, and Implications for Vaccine Development.Viruses · 2024Review
- A panel of hepatitis C virus glycoproteins for the characterization of antibody responses using antibodies with diverse recognition and neutralization patterns.Virus research · 2024Article
- Hepatitis C virus modified sE2Journal of virology · 2024Article
- Signatures of VNature communications · 2023Article
- Structure of engineered hepatitis C virus E1E2 ectodomain in complex with neutralizing antibodies.Nature communications · 2023Article
- Structures of the Hepaci-, Pegi-, and Pestiviruses envelope proteins suggest a novel membrane fusion mechanism.PLoS biology · 2023Article
- Current Hepatitis C Vaccine Candidates Based on the Induction of Neutralizing Antibodies.Viruses · 2023Review
- HCV E1 influences the fitness landscape of E2 and may enhance escape from E2-specific antibodies.Virus evolution · 2023Article
- Pseudotyped Virus for Flaviviridae.Advances in experimental medicine and biology · 2023Article
- Structure of the hepatitis C virus E1E2 glycoprotein complex.Science (New York, N.Y.) · 2022Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
13 authors at 5 institutions in 2 countries.
Funding
Abstract
The E1 and E2 envelope proteins of hepatitis C virus (HCV) form a heterodimer that drives virus-host membrane fusion. Here, we analyze the role of each amino acid in E1E2 function, expressing 545 individual alanine mutants of E1E2 in human cells, incorporating them into infectious viral pseudoparticles, and testing them against 37 different monoclonal antibodies (MAbs) to ascertain full-length translation, folding, heterodimer assembly, CD81 binding, viral pseudoparticle incorporation, and infectivity. We propose a model describing the role of each critical residue in E1E2 functionality and use it to examine how MAbs neutralize infection by exploiting functionally critical sites of vulnerability on E1E2. Our results suggest that E1E2 is a surprisingly fragile protein complex where even a single alanine mutation at 92% of positions disrupts its function. The amino-acid-level targets identified are highly conserved and functionally critical and can be exploited for improved therapies and vaccines.
Indexed as
Identifiers
What Socratic holds
Registered trials
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 Socratic graph.