Preliminary study on a potential antibacterial peptide derived from histone H2A in hemocytes of scallop Chlamys farreri
文献类型：期刊论文
| 作者 | Li, Chenghua; Song, Linsheng; Zhao, Jianmin; Zhu, Ling; Zou, Huibin; Zhang, Huan; Wang, Hao; Cai, Zhonghua |
| 刊名 | FISH & SHELLFISH IMMUNOLOGY
 |
| 出版日期 | 2007-06-01 |
| 卷号 | 22期号:6页码:663-672 |
| 关键词 | Chlamys Farreri Antibacterial Peptide Histone H2a Recombinant Product Antibacterial Activity |
| ISSN号 | 1050-4648 |
| DOI | 10.1016/j.fsi.2006.08.013 |
| 文献子类 | Article |
| 英文摘要 | Histone H2A is reported to participate in host defense response through producing novel antimicrobial peptides (AMPs) from its N-terminus in vertebrates and invertebrates, while the AMPs derived from H2A have not to our knowledge been reported in mollusca. In the present study, gene cloning, mRNA expression of H2A from scallop Chlamys farreri, and the recombinant expression of its N-terminus were conducted to investigate whether a similar mechanism exists in mollusca. The full-length DNA of H2A was identified by the techniques of homology cloning and genomic DNA walking, The full-length DNA of the scallop H2A was 696 bp long, including a 5'-terminal untranslated region (UTR) of 90 bp, a 3'-terminal UTR of 228 bp with a stem-loop structure and a canonical polyadenylation signal sequence AATAAA, and an open reading frame of 375 bp encoding a polypeptide of 125 amino acids. The mRNA expression of H2A in the hemocytes of scallop challenged by microbe was measured by semi-quantitative RT-PCR. The expression of H2A was not upregulated after stimulation, suggesting that H2A did not participate in immunity response directly. The DNA fragment of 117 bp encoding 39 amino acids corresponding to the N-terminus of scallop H2A, which was homologous to buforin I in vertebrates, was cloned into Pichia pastoris GS115. The transformants (His(+) Mut(+)) containing multi-copy gene insertion were selected with increasing concentration of antibiotic G418. The peptide of 39 amino acids was expressed by induction of 0.5% methanol. The recombinant product exerted antibacterial activity against both Gram-positive (G(+)) and Gram-negative (G(-)) bacteria. The antibacterial activity toward G(+) bacteria was 2.5 times more than that against G(-) bacteria. The results elucidated that N-terminus of H2A was a potential AMP and provided a promising candidate for a new antibiotic screening. However, whether H2A is really involved in scallop immune response mechanisms needs to be further investigated. (C) 2006 Elsevier Ltd. All rights reserved.; Histone H2A is reported to participate in host defense response through producing novel antimicrobial peptides (AMPs) from its N-terminus in vertebrates and invertebrates, while the AMPs derived from H2A have not to our knowledge been reported in mollusca. In the present study, gene cloning, mRNA expression of H2A from scallop Chlamys farreri, and the recombinant expression of its N-terminus were conducted to investigate whether a similar mechanism exists in mollusca. The full-length DNA of H2A was identified by the techniques of homology cloning and genomic DNA walking, The full-length DNA of the scallop H2A was 696 bp long, including a 5'-terminal untranslated region (UTR) of 90 bp, a 3'-terminal UTR of 228 bp with a stem-loop structure and a canonical polyadenylation signal sequence AATAAA, and an open reading frame of 375 bp encoding a polypeptide of 125 amino acids. The mRNA expression of H2A in the hemocytes of scallop challenged by microbe was measured by semi-quantitative RT-PCR. The expression of H2A was not upregulated after stimulation, suggesting that H2A did not participate in immunity response directly. The DNA fragment of 117 bp encoding 39 amino acids corresponding to the N-terminus of scallop H2A, which was homologous to buforin I in vertebrates, was cloned into Pichia pastoris GS115. The transformants (His(+) Mut(+)) containing multi-copy gene insertion were selected with increasing concentration of antibiotic G418. The peptide of 39 amino acids was expressed by induction of 0.5% methanol. The recombinant product exerted antibacterial activity against both Gram-positive (G(+)) and Gram-negative (G(-)) bacteria. The antibacterial activity toward G(+) bacteria was 2.5 times more than that against G(-) bacteria. The results elucidated that N-terminus of H2A was a potential AMP and provided a promising candidate for a new antibiotic screening. However, whether H2A is really involved in scallop immune response mechanisms needs to be further investigated. (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:000245918500008 |
| 公开日期 | 2010-12-24 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/5599]  |
| 专题 | 海洋研究所_实验海洋生物学重点实验室 |
| 作者单位 | 1.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Li, Chenghua,Song, Linsheng,Zhao, Jianmin,et al. Preliminary study on a potential antibacterial peptide derived from histone H2A in hemocytes of scallop Chlamys farreri[J]. FISH & SHELLFISH IMMUNOLOGY,2007,22(6):663-672. |
| APA | Li, Chenghua.,Song, Linsheng.,Zhao, Jianmin.,Zhu, Ling.,Zou, Huibin.,...&Cai, Zhonghua.(2007).Preliminary study on a potential antibacterial peptide derived from histone H2A in hemocytes of scallop Chlamys farreri.FISH & SHELLFISH IMMUNOLOGY,22(6),663-672. |
| MLA | Li, Chenghua,et al."Preliminary study on a potential antibacterial peptide derived from histone H2A in hemocytes of scallop Chlamys farreri".FISH & SHELLFISH IMMUNOLOGY 22.6(2007):663-672. |
入库方式： OAI收割
来源：海洋研究所
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。