ArticleBiochemistry and biophysics reports2016
A glucose/mannose binding lectin from litchi (
Article in Biochemistry and biophysics reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 26 citations in OpenAlex.
- Lectins as Natural Antibiofilm Agents in the Fight Against Antibiotic Resistance: A Review.Molecules (Basel, Switzerland) · 2025Review
- BOL Lectin: A Protein Derived from Cauliflower Exhibits Antibiofilm Activity in In Vitro Assays AgainstMicroorganisms · 2025Article
- Carbohydrate-Binding Mechanism of the Coagulant Lectin fromMolecules (Basel, Switzerland) · 2024Article
- Comprehensive Review on Fruit Seeds: Nutritional, Phytochemical, Nanotechnology, Toxicity, Food Biochemistry, and Biotechnology Perspective.Applied biochemistry and biotechnology · 2024Review
- Plant lectins as prospective antiviral biomolecules in the search for COVID-19 eradication strategies.Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie · 2022Review
- Potential Application of Combined Therapy with Lectins as a Therapeutic Strategy for the Treatment of Bacterial Infections.Antibiotics (Basel, Switzerland) · 2021Review
- Transcriptome Analysis Identified Coordinated Control of Key Pathways Regulating Cellular Physiology and Metabolism uponJournal of fungi (Basel, Switzerland) · 2020Article
- Microscopy examination of red blood and yeast cell agglutination induced by bacterial lectins.PloS one · 2019Article
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundLectins are highly important biomolecules to study several biological processes. A novel α-D-glucose/mannose specific lectin was isolated from the seeds of litchi fruits (
methodsPurification was done by successive Sephadex G 100 and Con A-Sepharose 4B affinity chromatography. SDS-PAGE, Surface Plasmon Resonance (SPR), steady state absorbance, fluorescence, time-correlated single-photon counting, circular dichroism and antibiofilm activity by measuring total protein estimation and azocasein degradation assay have been performed.
resultsThe purified lectin is a homodimer of molecular mass ~ 54 kDa. The amount of lectin required for hemagglutination of normal human O erythrocytes was 6.72 µg/ml. Among the saccharides tested, Man-α-(1,6)-Man was found to be the most potent inhibitor (0.01 mM) determined by hemagglutination inhibition assay. Steady state and time resolved fluorescence measurements revealed that litchi lectin formed ground state complex with maltose (K
conclusionsA novel homodimeric lectin has been purified from the seeds of litchi fruits ( GENERAL SIGNIFICANCE: The newly identified litchi lectin is highly specific for α-d-glucose/mannose with an important antibiofilm activity towards
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