Purification and characterization of a natural lectin from the plasma of the shrimp Fenneropenaeus chinensis

doi:10.1016/j.fsi.2008.06.001

	Purification and characterization of a natural lectin from the plasma of the shrimp Fenneropenaeus chinensis
	Sun, Jie 1,2; Wang, Lei 1; Wang, Baojie 1; Guo, Zhenyu 1; Liu, Mei 1; Jiang, Keyong 1; Tao, Ran 1,2; Zhang, Guofan 1
刊名	FISH & SHELLFISH IMMUNOLOGY
	2008-09-01
卷号	25 期号:3 页码:290-297
关键词	Affinity Chromatography Shrimp Lectin Invertebrate Pattern Recognition Protein
ISSN号	1050-4648
DOI	10.1016/j.fsi.2008.06.001
文献子类	Article
英文摘要	A natural lectin from the plasma of the shrimp Fenneropenaeus chinensis was purified by singlestep affinity chromatography using fetuin-coupled agarose. The purified plasma lectin showed a strong affinity for human A/B/O erythrocytes (RBC), mouse RBC and chicken RBC. The hemagglutinating (HA) activity of the lectin was dependent on Ca2+ and reversibly sensitive to EDTA. This lectin was named FC-L and its inactive form had a molecular mass estimate of 168 kDa. Fifteen N-terminal amino acid sequences of this protein were determined. We performed HA-inhibition assays with several carbohydrates and glycoproteins. FC-L showed a distinct and unique specificity to N-acetylated sugars, particularly sialic acid and sialoproteins. The FC-L also has binding activity to some Gram-negative bacteria which caused disease in shrimp and fish. The activity of FC-L was inhibited at temperatures greater than 75 degrees C and at a pH less than 7 or greater than 11. These results suggest that FC-L may play a role as pattern recognition proteins in the reorganization and clearance of invaders in shrimp F. chinensis. Crown Copyright (c) 2008 Published by Elsevier Ltd. All rights reserved.; A natural lectin from the plasma of the shrimp Fenneropenaeus chinensis was purified by singlestep affinity chromatography using fetuin-coupled agarose. The purified plasma lectin showed a strong affinity for human A/B/O erythrocytes (RBC), mouse RBC and chicken RBC. The hemagglutinating (HA) activity of the lectin was dependent on Ca2+ and reversibly sensitive to EDTA. This lectin was named FC-L and its inactive form had a molecular mass estimate of 168 kDa. Fifteen N-terminal amino acid sequences of this protein were determined. We performed HA-inhibition assays with several carbohydrates and glycoproteins. FC-L showed a distinct and unique specificity to N-acetylated sugars, particularly sialic acid and sialoproteins. The FC-L also has binding activity to some Gram-negative bacteria which caused disease in shrimp and fish. The activity of FC-L was inhibited at temperatures greater than 75 degrees C and at a pH less than 7 or greater than 11. These results suggest that FC-L may play a role as pattern recognition proteins in the reorganization and clearance of invaders in shrimp F. chinensis. Crown Copyright (c) 2008 Published by Elsevier Ltd. All rights reserved.
学科主题	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
URL标识	查看原文
语种	英语
WOS记录号	WOS:000259759700013
公开日期	2010-12-24
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/6093]
专题	海洋研究所_海洋生物技术研发中心
作者单位	1.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China
推荐引用方式 GB/T 7714	Sun, Jie,Wang, Lei,Wang, Baojie,et al. Purification and characterization of a natural lectin from the plasma of the shrimp Fenneropenaeus chinensis[J]. FISH & SHELLFISH IMMUNOLOGY,2008,25(3):290-297.
APA	Sun, Jie.,Wang, Lei.,Wang, Baojie.,Guo, Zhenyu.,Liu, Mei.,...&Zhang, Guofan.(2008).Purification and characterization of a natural lectin from the plasma of the shrimp Fenneropenaeus chinensis.FISH & SHELLFISH IMMUNOLOGY,25(3),290-297.
MLA	Sun, Jie,et al."Purification and characterization of a natural lectin from the plasma of the shrimp Fenneropenaeus chinensis".FISH & SHELLFISH IMMUNOLOGY 25.3(2008):290-297.