Bifunctional role of a pattern recognition molecule β-1,3 glucan binding protein purified from mangrove crab Episesarma tetragonum

被引：18
作者：
Sivakamavalli, Jeyachandran [1 ]
Vaseeharan, Baskaralingam [1 ]
机构：
[1] Alagappa Univ, Dept Anim Hlth & Management, Crustacean Mol Biol & Genom Lab, Karaikkudi 630004, Tamil Nadu, India
来源：
JOURNAL OF INVERTEBRATE PATHOLOGY | 2014年 / 119卷
关键词：
Agglutination; beta-Glucan binding protein; Episesarma tetragonum; Innate immunity; Prophenoloxidase; PLASMA-PROTEIN; TIGER SHRIMP; PROPHENOLOXIDASE; PURIFICATION; ACTIVATION; HEMOLYMPH; SYSTEM; IDENTIFICATION; SILKWORM; CLONING;
D O I：
10.1016/j.jip.2014.02.013
中图分类号：
Q95 [动物学];
学科分类号：
071002 ;
摘要：
beta-1,3-Glucan binding protein (beta-GBP) was purified from the haemolymph of Episesarma tetragonum by affinity chromatography with epoxy-activated laminarin-sepharose CL-6B column. E. tetragonum beta-GBP exhibits a single band with a molecular weight of 100 kDa on SDS-PAGE and a pI of 5.9 in isoelectric focusing (IEF). The circular dichroism (CD) spectra result of E. tetragonum beta-GBP indicates that the negative ellipticity bands near 220 nm and 208 nm correspond to the beta-sheets in the secondary structure. Functional analysis results demonstrate that the purified E. tetragonum beta-GBP agglutinates fungal cells (Candida albicans) containing p-glucan. This recognition and binding specificity leads to the activation of the prophenoloxidase (ProPO) cascade and enhance the phenoloxidase (PO) activity in a dose-dependent manner. Our finding discloses new insights in the ProPO activation and fungal agglutination of purified E. tetragonum beta-GBP. It seems to play a significant role in microbial uncovering mechanism in invertebrates. (C) 2014 Elsevier Inc. All rights reserved.
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页码：25 / 31
页数：7
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