Purification,characterization and induction of a C-type lectin in the freshwater planarian <Emphasis Type="Italic">Dugesia japonica</Emphasis> |
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Authors: | Qiuxiang Pang Xuemei Liu Bosheng Zhao Wei Wei Xiufang Zhang Lianfei Zhao Jingjing Xie Huanhuan Sun |
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Institution: | 1.School of Life Sciences,Shandong University of Technology,Zibo,China;2.Department of Nephrology, Affiliated Hospital of Medical College,Qingdao University,Qingdao,China |
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Abstract: | Lectins are important components of the immune defense system of invertebrates. Given their important functions, numerous
investigations have been carried out on the characterization and function of lectins in invertebrates. However, lectin studies
with the freshwater planarian, an evolutionarily important animal, are rare. In this paper, we demonstrate agglutination of
glutaraldehyde treated erythrocytes by a lectin with preference for rabbit erythrocytes. The result of hemagglutinating activity
inhibition assays with several carbohydrates showed the most potent inhibitor was maltose. A natural lectin from the crude
homogenates of freshwater planarian Dugesia japonica was purified by single step affinity chromatography using amylose-coupled agarose. The purified protein appeared as one band
with a molecular mass of 350 kDa in PAGE, and as one band, approximately 56 kDa, in SDS-PAGE. The purified lectin showed dependence
on calcium. The activity of the purified lectin was inhibited at temperatures greater than 50°C and showed a pH optimum between
5–8. The purified lectin also has binding activity to the Gram-negative bacteria E. coli, and the Gram-positive bacteria B. subtilis. Furthermore, the purified lectin obtained from injured and bacteria-induced planarians showed increased agglutinating activity
against rabbit erythrocytes. These results suggest that the purified lectin may play an important role in the innate immunity
of the freshwater planarian. |
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