Evidence map›Paper›PMID 25673725›Full record

ArticleJournal of virology2015

Monoclonal antibodies against extracellular domains of claudin-1 block hepatitis C virus infection in a mouse model.

Masayoshi Fukasawa, Shotaro Nagase, Yoshitaka Shirasago, Manami Iida, Mayo Yamashita, Kohki Endo, Kiyohito Yagi, Tetsuro Suzuki, Takaji Wakita, Kentaro Hanada and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

28 citing papers in PubMed, 52 citations in OpenAlex.

  1. Review
  2. Antiviral Protein-Protein Interaction Inhibitors.Journal of medicinal chemistry · 2024
    Review
  3. Article
  4. Association of Plasma Claudin-5 with Age and Alzheimer Disease.International journal of molecular sciences · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Hepatitis C virus infection and tight junction proteins: The ties that bind.Biochimica et biophysica acta. Biomembranes · 2020
    Review
  11. Article
  12. Claudin-1, A Double-Edged Sword in Cancer.International journal of molecular sciences · 2020
    Review
  13. Review
  14. Article
  15. Use of ModifiedInternational journal of molecular sciences · 2019
    Article
  16. Review
  17. Review
  18. Article
  19. Mouse Models for Studying HCV Vaccines and Therapeutic Antibodies.Methods in molecular biology (Clifton, N.J.) · 2019
    Article
  20. Article
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.

Masayoshi FukasawaDepartment of Biochemistry and Cell Biology, National Institute of Infectious Diseases, Tokyo, Japan fuka@nih.go.jp masuo@phs.osaka-u.ac.jp.
Shotaro NagaseLaboratory of Bio-Functional Molecular Chemistry, Graduate School of Pharmaceutical Sciences, Osaka University, Osaka, Japan.
Yoshitaka ShirasagoDepartment of Biochemistry and Cell Biology, National Institute of Infectious Diseases, Tokyo, Japan Graduate School of Biological Science, Tokyo University of Science, Chiba, Japan.
Manami IidaLaboratory of Bio-Functional Molecular Chemistry, Graduate School of Pharmaceutical Sciences, Osaka University, Osaka, Japan.
Mayo YamashitaLaboratory of Bio-Functional Molecular Chemistry, Graduate School of Pharmaceutical Sciences, Osaka University, Osaka, Japan.
Kohki EndoLife Science Research Laboratories, Wako Pure Chemical Industries, Ltd., Hyogo, Japan.
Kiyohito YagiLaboratory of Bio-Functional Molecular Chemistry, Graduate School of Pharmaceutical Sciences, Osaka University, Osaka, Japan.
Tetsuro SuzukiDepartment of Infectious Diseases, Hamamatsu University School of Medicine, Shizuoka, Japan.
Takaji WakitaDepartment of Virology II, National Institute of Infectious Diseases, Tokyo, Japan.
Kentaro HanadaDepartment of Biochemistry and Cell Biology, National Institute of Infectious Diseases, Tokyo, Japan.
Hiroki KuniyasuDepartment of Molecular Pathology, Nara Medical University, Nara, Japan.
Masuo KondohLaboratory of Bio-Functional Molecular Chemistry, Graduate School of Pharmaceutical Sciences, Osaka University, Osaka, Japan fuka@nih.go.jp masuo@phs.osaka-u.ac.jp.
Osaka University · JPNational Institute of Infectious Diseases · JPHamamatsu University School of Medicine · JPNara Medical University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

unlabelledHepatitis C virus (HCV) entry into host cells is a complex process requiring multiple host factors, including claudin-1 (CLDN1). Safe and effective therapeutic entry inhibitors need to be developed. We isolated a human hepatic Huh7.5.1-derived cell mutant that is nonpermissive to HCV, and comparative microarray analysis showed that the mutant was CLDN1 defective. Four hybridomas were obtained, which produced monoclonal antibodies (MAbs) that interacted with the parental Huh7.5.1 cell but not with the CLDN1-defective mutant. All MAbs produced by these hybridomas specifically bound to human CLDN1 with a very high affinity and prevented HCV infection of Huh7.5.1 cells in a dose-dependent manner, without apparent cytotoxicity. Two selected MAbs also inhibited HCV infection of human liver-chimeric mice without significant adverse effects. CLDN1 may be a potential target to prevent HCV infection in vivo. Anti-CLDN1 MAbs may hence be promising candidates as novel anti-HCV agents. IMPORTANCE: Safe and effective therapeutic entry inhibitors against hepatitis C virus (HCV) are very useful for combination therapies with other anti-HCV drugs, such as direct-acting antivirals. In this study, we first showed an effective strategy for developing functional monoclonal antibodies (MAbs) against extracellular domains of a multimembrane-spanning target protein, claudin-1 (CLDN1), by using parental cells expressing the intact target membrane protein and target-defective cells. The established MAbs against CLDN1, which had a very high affinity for intact CLDN1, efficiently inhibited in vitro and in vivo HCV infections. These anti-CLDN1 MAbs are promising leads for novel entry inhibitors against HCV.

Indexed as

AnimalsAntibodies, MonoclonalCell LineClaudin-1Disease Models, AnimalDrug-Related Side Effects and Adverse ReactionsHepacivirusHepatitis CHepatocytesHumansMaleMiceReceptors, VirusTreatment OutcomeVirus InternalizationAntibodies, MonoclonalClaudin-1CLDN1 protein, humanReceptors, Virus

Identifiers

PMID25673725
PMCPMC4403477
OpenAlexW2050157665

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.