A lectin with anti-microbial and anti proliferative activities from Lantana camara, a medicinal plant
Autor: | Supreeth S. Kulkarni, Shivakumar Belur, Kavita Y. Hiremath, Shashikala R. Inamdar, Narasimhappagari Jagadeesh |
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Rok vydání: | 2019 |
Předmět: |
0106 biological sciences
Antifungal Agents Lantana camara Ion chromatography Size-exclusion chromatography Lantana Antineoplastic Agents Chitin Microbial Sensitivity Tests 01 natural sciences Chromatography Affinity Sepharose 03 medical and health sciences Affinity chromatography 010608 biotechnology Gram-Negative Bacteria Humans IC50 030304 developmental biology Melibiose 0303 health sciences Plants Medicinal biology Chemistry Plant Extracts Mucin Fungi Mucins Lectin biology.organism_classification Chromatography Ion Exchange Methylgalactosides Anti-Bacterial Agents Plant Leaves Biochemistry biology.protein Chromatography Gel Electrophoresis Polyacrylamide Gel Plant Lectins HT29 Cells Biotechnology Protein Binding |
Zdroj: | Protein expression and purification. 170 |
ISSN: | 1096-0279 |
Popis: | Background Lectins are known to possess interesting biological properties such as anti microbial, nematicidal, anti tumor and anti viral activities. Lantana camara from verbenaceae family is a medicinal plant known for possessing anti oxidant and anticancer activities. Since anticancer activity is reported in plant lectins, leaves of Lantana camara was used to check the presence of lectin. Methods and results Here we report the purification, characterization and biological properties of a lectin from Lantana camara (LCL) leaves. LCL was purified by ion exchange chromatography on CM-cellulose column followed by affinity chromatography on mucin coupled Sepharose 4B column and gel filtration chromatography on Superdex G75 column. LCL is a glycoprotein with 10% of the carbohydrate and is blood group non specific. SDS-PAGE analysis of affinity purified LCL showed two proteins with apparent molecular weight of 14.49 kDa and 17.4 kDa which were subsequently separated by Gel filtration chromatography on Superdex G75 column. Hapten inhibition studies of LCL revealed its highest affinity for Chitin, Milibiose, α-D-Methyl galactopyranoside and glycoproteins like mucin, asialomucin. LCL showed strong binding to human colon adenocarcinoma HT29 cells with MFI of 242 which was effectively blocked by 68.1 and 62.5% by both mucin and milibiose. LCL showed dose and time dependent growth inhibitory effects on HT29 cells with IC50 of 3.75 μg/ml at 48 h. LCL has potent antibacterial and anti fungal activity. Conclusion LCL can be explored for its clinical potential. |
Databáze: | OpenAIRE |
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