| 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 | |
| 2007-08-01 | |
| 发表期刊 | FISH & SHELLFISH IMMUNOLOGY
 |
| ISSN | 1050-4648 |
| 卷号 | 23期号:2页码:292-299 |
| 文章类型 | Article |
| 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. |
| 关键词 | Affinity Chromatography Shrimp Acetyl Group Specificity Lectin Invertebrate |
| 学科领域 | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| DOI | 10.1016/j.fsi.2006.11.001 |
| URL | 查看原文 |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000247309300005 |
| 引用统计 | |
| 文献类型 | 期刊论文 |
| 条目标识符 | http://ir.qdio.ac.cn/handle/337002/6090 |
| 专题 | 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. |
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