Isolation, purification and characterization of beta-1,3-glucan binding protein from the plasma of marine mussel Perna viridis

Fish & Shellfish Immunology
S S JayarajP Mullainadhan

Abstract

A beta-1,3-glucan binding protein (betaGBP) specific for laminarin (a beta-1,3-glucan) was detected for the first time in a mollusc, Perna viridis. betaGBP was isolated and purified from the plasma using laminarin precipitation and affinity chromatography on laminarin-Sepharose 6B, respectively. It agglutinated bakers yeast, bacteria, and erythrocytes and enhanced prophenoloxidase (proPO) activity of the plasma in a dose-dependent manner. The purified betaGBP appeared as a single band in native-PAGE and the purity was conformed by HPLC. The protein has a molecular weight estimate of 510kDa as determined by SDS-PAGE and in isoelectric focusing the purified betaGBP was focused as a single band at pI 5.3. betaGBP was found to possess inherent serine protease activity but lacked beta-1,3-glucanase activity and all these results suggest that plasma betaGBP of P. viridis functions as a recognition molecule for beta-1,3-glucan on the surface of microbial cell walls. This recognition and binding lead to the activation of the prophenoloxidase cascade mediated by the inherent serine protease activity of betaGBP. Presence of agglutinating activity and serine protease activity shows that betaGBP is a bifunctional protein. The findings are ...Continue Reading

Citations

Apr 1, 2014·Journal of Invertebrate Pathology·Jeyachandran Sivakamavalli, Baskaralingam Vaseeharan
Jul 6, 2014·Developmental and Comparative Immunology·Jianfeng DingXiwu Yan
Feb 18, 2016·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·Ximing Guo, Susan E Ford
Feb 7, 2016·Fish & Shellfish Immunology·Mausumi Adhya, Biswajit Singha
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Mar 8, 2018·International Journal of Molecular Sciences·Weilin WangLinsheng Song
Jan 19, 2019·PloS One·Anna Przekoracka-KrawczykPaulina Pyżalska

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