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Purification, characterization and functional analysis of a novel β-1, 3-glucan binding protein from green tiger shrimp Penaeus semisulcatus.
- Source :
-
Fish & Shellfish Immunology . Sep2013, Vol. 35 Issue 3, p689-696. 8p. - Publication Year :
- 2013
-
Abstract
- Abstract: 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. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 10504648
- Volume :
- 35
- Issue :
- 3
- Database :
- Academic Search Index
- Journal :
- Fish & Shellfish Immunology
- Publication Type :
- Academic Journal
- Accession number :
- 89975969
- Full Text :
- https://doi.org/10.1016/j.fsi.2013.05.017