Purification, characterization and functional analysis of a novel β-1, 3-glucan binding protein from green tiger shrimpPenaeus semisulcatus

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A β-1, 3-Glucan binding protein (β-GBP) was isolated from green tiger shrimp Penaeus semisulcatus and purified using laminarin precipitation and affinity chromatography on laminarin-Sepharose 6B column respectively. P. semisulcatus β-GBP exhibits a single band with a molecular weight of 112 kDa on SDS-PAGE and pI of 5.9 in isoelectric focusing (IEF). Negative staining of P. semisulcatus β-GBP showed large aggregates with crystalline surface when viewed by Electron Microscopy. Circular dichroism spectra of P. semisulcatus β-GBP showed broad negative minimum wavelength extending from 200 to 250 nm can be attributed to the presence of β-sheets in its secondary structure. P. semisulcatus β-GBP comprises the specific binding affinity with the polysaccharide β-1, 3-glucans (laminarin), this recognition and binding leads to the activation of prophenoloxidase cascade. Interestingly, P. semisulcatus β-GBP also involved in the agglutination of baker's yeast, bacteria, erythrocytes (RBCs) and enhances the PO activity. Herein, we have investigated the importance of β-GBP in innate immune response of P. semisulcatus and they implicate the evolutionary link with similar proteins found in other invertebrates.HighlightsWe have purified the β-GBP from the plasma of Penaeus semisulcatus by affinity chromatography.Purified P. semisulcatus β-GBP molecular weight of 112 kDa on SDS-PAGE and pI of 5.9 in IEF.Secondary and surface analysis of P. semisulcatus β-GBP was investigated by CD, TEM characterization.P. semisulcatus β-GBP showed agglutination of yeast, bacteria, RBC and enhanced the PO activity.

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