Evidence map›Paper›PMID 24152340›Full record

ArticleMolecular pharmaceutics2013

Inhibition of hepatitis C virus by the cyanobacterial protein Microcystis viridis lectin: mechanistic differences between the high-mannose specific lectins MVL, CV-N, and GNA.

Alla Kachko, Sandra Loesgen, Syed Shahzad-Ul-Hussan, Wendy Tan, Iryna Zubkova, Kazuyo Takeda, Frances Wells, Steven Rubin, Carole A Bewley, Marian E Major

Open access · greenAbstract read
In one paragraph

Article in Molecular pharmaceutics, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

27 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
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  5. Lectins and lectibodies: potential promising antiviral agents.Cellular & molecular biology letters · 2022
    Review
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  12. Antimicrobial agents and chemotherapy · 2021
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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

10 authors at 4 institutions in 1 country.

Alla Kachko *Laboratory of Hepatitis Viruses, Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892 USA.
Sandra Loesgen *Laboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda Maryland 20892, USA.
Syed Shahzad-Ul-HussanLaboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda Maryland 20892, USA.
Wendy TanLaboratory of Hepatitis Viruses, Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892 USA.
Iryna ZubkovaLaboratory of Hepatitis Viruses, Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892 USA.
Kazuyo TakedaMicroscopy and Imaging Core Facility, Center for Biologics Evaluation and Research, US Food and Drug Administration, Bethesda, MD 20892. USA.
Frances WellsLaboratory of Hepatitis Viruses, Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892 USA.
Steven RubinLaboratory of Method Development, Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892. USA.
Carole A BewleyLaboratory of Bioorganic Chemistry, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda Maryland 20892, USA.
Marian E MajorLaboratory of Hepatitis Viruses, Division of Viral Products, Center for Biologics Evaluation and Research, Food and Drug Administration, Bethesda, MD 20892 USA.
National Institutes of Health · USNational Institute of Allergy and Infectious Diseases · USNational Institute of Diabetes and Digestive and Kidney Diseases · USUnited States Food and Drug Administration · US

Funding

Discovery, Structural Studies and Biosynthesis of Biologically Active Natural Products and Natural Product-Like InhibitorsZIADK031135 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BEWLEY, CAROLE · 2009 to 2025
$16.9M
Inhibitors and Probes of HIV-1 Cell FusionZIADK032103 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BEWLEY, CAROLE · 2009 to 2025
$12.5M
Inhibitors Of Hiv-1 Cell Fusion And Mycothiol-related EnZ01DK032103 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BEWLEY, CAROLE · 2000 to 2008
$896k
Discovery of Natural Products and Natural Product-Like InhibitorsZ01DK031135 · NIDDK · NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES · PI BEWLEY, CAROLE · 2007 to 2008
$844k
Intramural NIH HHS Z01 DK032103Intramural NIH HHS ZIA DK032103
6 · The paper itself

Abstract

Plant or microbial lectins are known to exhibit potent antiviral activities against viruses with glycosylated surface proteins, yet the mechanism(s) by which these carbohydrate-binding proteins exert their antiviral activities is not fully understood. Hepatitis C virus (HCV) is known to possess glycosylated envelope proteins (gpE1E2) and to be potently inhibited by lectins. Here, we tested in detail the antiviral properties of the newly discovered Microcystis viridis lectin (MVL) along with cyanovirin-N (CV-N) and Galanthus nivalis agglutinin (GNA) against cell culture HCV, as well as their binding properties toward viral particles, target cells, and recombinant HCV glycoproteins. Using infectivity assays, CV-N, MVL, and GNA inhibited HCV with IC50 values of 0.6 nM, 30.4 nM, and 11.1 nM, respectively. Biolayer interferometry analysis demonstrated a higher affinity of GNA to immobilized recombinant HCV glycoproteins compared to CV-N and MVL. Complementary studies, including fluorescence-activated cell sorting (FACS) analysis, confocal microscopy, and pre- and post-virus binding assays, showed a complex mechanism of inhibition for CV-N and MVL that includes both viral and cell association, while GNA functions by binding directly to the viral particle. Combinations of GNA with CV-N or MVL in HCV infection studies revealed synergistic inhibitory effects, which can be explained by different glycan recognition profiles of the mainly high-mannoside specific lectins, and supports the hypothesis that these lectins inhibit through different and complex modes of action. Our findings provide important insights into the mechanisms by which lectins inhibit HCV infection. Overall, the data suggest MVL and CV-N have the potential for toxicity due to interactions with cellular proteins while GNA may be a better therapeutic agent due to specificity for the HCV gpE1E2.

Indexed as

Antiviral AgentsBacterial ProteinsCarrier ProteinsCell Line, TumorCyanobacteriaGlycoproteinsHepacivirusHumansMannose-Binding LectinsMicrocystisPlant LectinsRecombinant ProteinsAntiviral AgentsBacterial ProteinsCarrier Proteinscyanovirin NGlycoproteinsMannose-Binding LectinsPlant LectinsRecombinant Proteinssnowdrop lectin

Identifiers

PMID24152340
PMCPMC3907190
OpenAlexW2092014032

What OpenQuestion holds

Textmetadata
LicenceTDM
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.