Evidence map›Paper›PMID 36137152›Full record

ArticlePloS one2022

Patient-derived monoclonal antibody neutralizes HCV infection in vitro and vivo without generating escape mutants.

Hiroshi Yokokawa, Midori Shinohara, Yuji Teraoka, Michio Imamura, Noriko Nakamura, Noriyuki Watanabe, Tomoko Date, Hideki Aizaki, Tomokatsu Iwamura, Hideki Narumi and 2 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Review
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

12 authors at 4 institutions in 1 country.

Hiroshi YokokawaPharmaceutical Research Laboratory, Toray Industries, Inc., Kanagawa, Japan.ORCID 0000-0002-3384-7043
Midori ShinoharaMedical & Biological Laboratories Co., Ltd., Tokyo, Japan.
Yuji TeraokaDepartment of Gastroenterology and Metabolism, Graduate School of Biomedical and Health Science, Hiroshima University, Hiroshima, Japan.
Michio ImamuraDepartment of Gastroenterology and Metabolism, Graduate School of Biomedical and Health Science, Hiroshima University, Hiroshima, Japan.
Noriko NakamuraPharmaceutical Research Laboratory, Toray Industries, Inc., Kanagawa, Japan.
Noriyuki WatanabeDepartment of Virology II, National Institute of Infectious Diseases, Tokyo, Japan.
Tomoko DateDepartment of Virology II, National Institute of Infectious Diseases, Tokyo, Japan.
Hideki AizakiDepartment of Virology II, National Institute of Infectious Diseases, Tokyo, Japan.
Tomokatsu IwamuraPharmaceutical Research Laboratory, Toray Industries, Inc., Kanagawa, Japan.
Hideki NarumiPharmaceutical Research Laboratory, Toray Industries, Inc., Kanagawa, Japan.
Kazuaki ChayamaResearch Center for Hepatology and Gastroenterology, Hiroshima University, Hiroshima, Japan.ORCID 0000-0002-5530-5341
Takaji WakitaDepartment of Virology II, National Institute of Infectious Diseases, Tokyo, Japan.
National Institute of Infectious Diseases · JPHiroshima University · JPToray Industries, Inc. (Japan) · JPMedical & Biological Laboratories (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In recent years, new direct-acting antivirals for hepatitis C virus (HCV) have been approved, but hepatitis C continues to pose a threat to human health. It is important to develop neutralizing anti-HCV antibodies to prevent medical and accidental infection, such as might occur via liver transplantation of chronic HCV patients and needle-stick accidents in the clinic. In this study, we sought to obtain anti-HCV antibodies using phage display screening. Phages displaying human hepatocellular carcinoma patient-derived antibodies were screened by 4 rounds of biopanning with genotype-1b and -2a HCV envelope E2 protein adsorbed to magnetic beads. The three antibodies obtained from this screen had reactivity against E2 proteins derived from both genotype-1b and -2a strains. However, in epitope analysis, these antibodies did not recognize linear peptides from an overlapping E2 epitope peptide library, and did not bind to denatured E2 protein. In addition, these antibodies showed cross-genotypic neutralizing activity against genotype-1a, -1b, -2a, and -3a cell culture-generated infectious HCV particles (HCVcc). Moreover, emergence of viral escape mutants was not observed after repeated rounds of passaging of HCV-infected cells in the presence of one such antibody, e2d066. Furthermore, injection of the e2d066 antibody into human hepatocyte-transplanted immunodeficient mice inhibited infection by J6/JFH-1 HCVcc. In conclusion, we identified conformational epitope-recognizing, cross-genotypic neutralizing antibodies using phage display screening. Notably, e2d066 antibody did not select for escape mutant emergence in vitro and demonstrated neutralizing activity in vivo. Our results suggested that these antibodies may serve as prophylactic and therapeutic agents.

Indexed as

Hepatitis CHepatitis C, ChronicAnimalsAntibodies, MonoclonalAntibodies, NeutralizingAntiviral AgentsEpitopesHepacivirusHepatitis C AntibodiesHumansMicePeptide LibraryViral Envelope ProteinsAntibodies, MonoclonalAntibodies, NeutralizingAntiviral AgentsEpitopesHepatitis C AntibodiesPeptide LibraryViral Envelope Proteins

Identifiers

PMID36137152
PMCPMC9499215
OpenAlexW4296804104

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.