ArticleViruses2020
An Engineered Microvirin Variant with Identical Structural Domains Potently Inhibits Human Immunodeficiency Virus and Hepatitis C Virus Cellular Entry.
Article in Viruses, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The trial behind it
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Who cites it
9 citing papers in PubMed.
- Engineering Protein-Based HIV Entry Inhibitors: Advances, Challenges, and Translational Strategies.Biomolecules · 2026Review
- Bridging Viral Glycobiology and Lectin Biotechnology for Antiviral and Diagnostic Strategies.ACS bio & med chem Au · 2025Review
- Mannose-specific plant and microbial lectins as antiviral agents: A review.Glycoconjugate journal · 2024Review
- The Antiviral Potential of Algal Lectins.Marine drugs · 2023Review
- Cyanometabolites: molecules with immense antiviral potential.Archives of microbiology · 2023Review
- Therapeutic Potential of Marine Bioactive Peptides against Human Immunodeficiency Virus: Recent Evidence, Challenges, and Future Trends.Marine drugs · 2022Review
- Legume Lectins with Different Specificities as Potential Glycan Probes for Pathogenic Enveloped Viruses.Cells · 2022Review
- Antiviral Cyanometabolites-A Review.Biomolecules · 2021Review
- Antiviral Agents: Discovery to Resistance.Viruses · 2020Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Microvirin (MVN) is one of the human immunodeficiency virus (HIV-1) entry inhibitor lectins, which consists of two structural domains sharing 35% sequence identity and contrary to many other antiviral lectins, it exists as a monomer. In this study, we engineered an MVN variant, LUMS1, consisting of two domains with 100% sequence identity, thereby reducing the chemical heterogeneity, which is a major factor in eliciting immunogenicity. We determined carbohydrate binding of LUMS1 through NMR chemical shift perturbation and tested its anti-HIV activity in single-round infectivity assay and its anti-hepatitis C virus (HCV) activity in three different assays including HCVcc, HCVpp, and replicon assays. We further investigated the effect of LUMS1 on the activation of T helper (T
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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 OpenQuestion graph.