ArticlePloS one2014
Purification and characterization of a mucin specific mycelial lectin from Aspergillus gorakhpurensis: application for mitogenic and antimicrobial activity.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 45 citations in OpenAlex.
- Article
- A Review of the Leishmanicidal Properties of Lectins.Current protein & peptide science · 2024Review
- Antimicrobial Studies on Garlic Lectin.Probiotics and antimicrobial proteins · 2023Article
- Article
- Expression of a Fungal Lectin in Arabidopsis Enhances Plant Growth and Resistance Toward Microbial Pathogens and a Plant-Parasitic Nematode.Frontiers in plant science · 2021Article
- An overview of lectin-glycan interactions: a key event in initiating fungal infection and pathogenesis.Archives of microbiology · 2018Review
- An update of the recombinant protein expression systems of Cyanovirin-N and challenges of preclinical development.BioImpacts : BI · 2018Review
- A detection and quantification label-free tool to speed up downstream processing of model mucins.PloS one · 2018Article
- Lectins, Interconnecting Proteins with Biotechnological/Pharmacological and Therapeutic Applications.Evidence-based complementary and alternative medicine : eCAM · 2017Review
- Lectins with anti-HIV activity: a review.Molecules (Basel, Switzerland) · 2015Review
- Lectin activity in mycelial extracts of Fusarium species.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology]Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundLectins are carbohydrate binding proteins or glycoproteins that bind reversibly to specific carbohydrates present on the apposing cells, which are responsible for their ability to agglutinate red blood cells, lymphocytes, fibroblasts, etc. Interest in lectins has been intensified due to their carbohydrate specificity as they can be valuable reagents for the investigation of cell surface sugars, purification and characterization of glycoproteins. The present study reports the purification, characterization and evaluation of mitogenic and antimicrobial potential of a mycelial lectin from Aspergillus gorakhpurensis.
methodsAffinity chromatography on mucin-sepharose column was carried out for purification of Aspergillus gorakhpurensis lectin. The lectin was characterized for physico-chemical parameters. Mitogenic potential of the lectin was evaluated against splenocytes of Swiss albino mice by MTT assay. Antimicrobial activity of the purified lectin has also been evaluated by disc diffusion assay.
resultsSingle-step affinity purification resulted in 18.6-fold purification of the mycelial lectin. The molecular mass of the lectin was found to be 70 kDa and it was composed of two subunits of 34.8 kDa as determined by gel filtration chromatography, SDS-PAGE and MALDI-TOF analysis. pH optima of the lectin was found to be 6.5-9.5, while optimum temperature for lectin activity was 20-30 °C. Lectin was stable within a pH range of 7.0-10.5 and showed fair thermostability. EDTA did not affect lectin activity whereas it was found susceptible to the denaturants tested. MTT assay revealed strong mitogenic potential of A. gorakhpurensis lectin at a concentration upto 150 µg/mL. Antimicrobial activity assay showed its potent antibacterial activity against Bacillus cereus, Staphylococcous aureus and Escherichia coli and marginal antifungal activity against Saccharomyces cerevisiae.
conclusionThis is the first report on the mitogenic and antimicrobial potential of Aspergillus gorakhpurensis lectin. The results will provide useful guidelines for further research in clinical applications of this lectin.
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