Purification and characterisation of a natural lectin from the serum of the shrimp Litopenaeus vannamei

doi:10.1016/j.fsi.2006.11.001

	Purification and characterisation of a natural lectin from the serum of the shrimp Litopenaeus vannamei
	Sun, Jie ; Wang, Lei ; Wang, Baojie ; Guo, Zhenyu ; Liu, Mei ; Jiang, Keyong ; Luo, Zuoyong
刊名	FISH & SHELLFISH IMMUNOLOGY
	2007-08-01
卷号	23 期号:2 页码:292-299
关键词	Affinity Chromatography Shrimp Acetyl Group Specificity Lectin Invertebrate
ISSN号	1050-4648
DOI	10.1016/j.fsi.2006.11.001
文献子类	Article
英文摘要	A natural lectin from the serum of the shrimp Litopenaeus vannamei was purified to homogeneity by a single-step affinity chromatography using fetuin-coupled agarose. The purified serum lectin (named LVL) showed a strong affinity for human A/B/O erythrocytes (RBC), mouse RBC, chicken RBC and its haemagglutinating (HA) activity was specifically dependent on Ca2+ and reversibly sensitive to EDTA. LVL inactive form had a molecular mass estimate of 172 kDa and was composed of two non-identical subunits (32 and 38 kDa) cross-linked by interchain disulphide bonds. Significant LVL activity was observed between pH 7 and 11. In HA-inhibition assays performed with several carbohydrates and glycoproteins, LVL showed a distinct and unique specificity for GalNAc/GluNAc/NeuAc which had an acetyl group, while glycoproteins fetuin and bovine submaxillary mucin (BSM) had sialic acid. Moreover, this agglutinin appeared to recognise the terminal N- and O-acetyl groups in the oligosaccharide chain of glycoconjugates. The HA activity of L. vannamei lectin was also susceptible to inhibition by lipopolysaccharides from diverse Gram-negative bacteria, which might indicate a significant in vivo role of this humoral agglutinin in the host immune response against bacterial infections. (C) 2006 Elsevier Ltd. All rights reserved.; A natural lectin from the serum of the shrimp Litopenaeus vannamei was purified to homogeneity by a single-step affinity chromatography using fetuin-coupled agarose. The purified serum lectin (named LVL) showed a strong affinity for human A/B/O erythrocytes (RBC), mouse RBC, chicken RBC and its haemagglutinating (HA) activity was specifically dependent on Ca2+ and reversibly sensitive to EDTA. LVL inactive form had a molecular mass estimate of 172 kDa and was composed of two non-identical subunits (32 and 38 kDa) cross-linked by interchain disulphide bonds. Significant LVL activity was observed between pH 7 and 11. In HA-inhibition assays performed with several carbohydrates and glycoproteins, LVL showed a distinct and unique specificity for GalNAc/GluNAc/NeuAc which had an acetyl group, while glycoproteins fetuin and bovine submaxillary mucin (BSM) had sialic acid. Moreover, this agglutinin appeared to recognise the terminal N- and O-acetyl groups in the oligosaccharide chain of glycoconjugates. The HA activity of L. vannamei lectin was also susceptible to inhibition by lipopolysaccharides from diverse Gram-negative bacteria, which might indicate a significant in vivo role of this humoral agglutinin in the host immune response against bacterial infections. (C) 2006 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:000247309300005
公开日期	2010-12-24
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/6091]
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, Shandong 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 characterisation of a natural lectin from the serum of the shrimp Litopenaeus vannamei[J]. FISH & SHELLFISH IMMUNOLOGY,2007,23(2):292-299.
APA	Sun, Jie.,Wang, Lei.,Wang, Baojie.,Guo, Zhenyu.,Liu, Mei.,...&Luo, Zuoyong.(2007).Purification and characterisation of a natural lectin from the serum of the shrimp Litopenaeus vannamei.FISH & SHELLFISH IMMUNOLOGY,23(2),292-299.
MLA	Sun, Jie,et al."Purification and characterisation of a natural lectin from the serum of the shrimp Litopenaeus vannamei".FISH & SHELLFISH IMMUNOLOGY 23.2(2007):292-299.