Antimicrobial properties and phenoloxidase activation of the lectin isolated from kadal shrimp (Metapenaeus dobsoni)

The present study reveals purification and characterization of the lectin from the haemolymph of Metapenaeus dobsoni. The Md-Lec was purified by affinity chromatography with mannose coupled sepharose CL-4B column and it exhibits single band with a molecular weight of 68 kDa in SDS-PAGE. Furthermore,...

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Bibliographic Details
Published in:Fish & shellfish immunology 2019-07, Vol.90, p.118-125
Main Authors: Rubeena, Abdul Salam, Preetham, Elumalai
Format: Article
Language:English
Subjects:
Antibacterial activity
Antiviral activity
Haemagglutination
Lectin
Metapenaeus dobsoni
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Summary:The present study reveals purification and characterization of the lectin from the haemolymph of Metapenaeus dobsoni. The Md-Lec was purified by affinity chromatography with mannose coupled sepharose CL-4B column and it exhibits single band with a molecular weight of 68 kDa in SDS-PAGE. Furthermore, the molecular mass was confirmed by MALDI-TOF and functional groups present were analysed by FTIR. The surface morphology of purified Md-Lec displays the homogeneous nature of protein. The X-ray diffraction (XRD) analysis expresses three peaks at 10.7716̊, 21.6258̊ and 31.7523̊which indicate the crystalline nature of the protein and the retention time of 3.068 min evident from HPLC reveals the purity of the sample. Functional analysis of purified Md-Lec exhibits yeast agglutination activity against Saccharomyces cerevisiae and has the ability to agglutinate the human erythrocytes, which was observed by light microscopy. It also exhibited phenoloxidase activation, encapsulation and phagocytic activities. In addition, purified Md-Lec showed the broad spectrum of bacterial agglutination activity against Gram negative Vibrio parahaemolyticus and Aeromonas hydrophila, important fish pathogens. •A lectin with a molecular mass of 68 kDa was purified and characterized from the haemolymph of Metapenaeus dobsoni.•Biochemical characterization was done by SDS-PAGE, XRD, FTIR, MALDI-TOF and HPLC.•Functional properties include haemagglutination, yeast agglutination and bacterial agglutination activities.•The purified lectin also exhibited significant antiviral activity, encapsulation activity and PO activity.
ISSN:1050-4648
1095-9947
DOI:10.1016/j.fsi.2019.04.305