| Purification and characterization of a natural lectin from the plasma of the shrimp Fenneropenaeus chinensis | |
| Sun, Jie1,2; Wang, Lei1; Wang, Baojie1; Guo, Zhenyu1; Liu, Mei1; Jiang, Keyong1; Tao, Ran1,2; Zhang, Guofan1 | |
| 2008-09-01 | |
| 发表期刊 | FISH & SHELLFISH IMMUNOLOGY
 |
| ISSN | 1050-4648 |
| 卷号 | 25期号:3页码:290-297 |
| 文章类型 | Article |
| 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. |
| 关键词 | Affinity Chromatography Shrimp Lectin Invertebrate Pattern Recognition Protein |
| 学科领域 | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| DOI | 10.1016/j.fsi.2008.06.001 |
| URL | 查看原文 |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000259759700013 |
| 引用统计 | |
| 文献类型 | 期刊论文 |
| 条目标识符 | http://ir.qdio.ac.cn/handle/337002/6092 |
| 专题 | 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. |
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