Molecular cloning and characterization of novel cathelicidin-derived myeloid antimicrobial peptide from Phasianus colchicus
Wang, Yipeng ; Lu, Zekuan ; Feng, Feifei ; Zhu, Wei ; Guang, Huijuan ; Liu, Jingze ; He, Weiyu ; Chi, Lianli ; Li, Zheng ; Yu, Haining
刊名DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
2011
卷号35期号:3页码:314-322
关键词Cathelicidin Phasianus Colchicus Pc-caths Antimicrobial Killing Kinetics Bovine Neutrophils Airway Epithelia Innate Immunity Rhesus-monkey Identification Bactenecins Expression Family Purification Antibiotics
ISSN号0145-305X
通讯作者Yu, HN, Hebei Normal Univ, Coll Life Sci, Shijiazhuang 050016, Hebei, Peoples R China.lianlichi@sdu.edu.cn ; joannyu@live.cn
产权排序[Lu, Zekuan; Feng, Feifei; Zhu, Wei; Liu, Jingze; He, Weiyu; Yu, Haining] Hebei Normal Univ, Coll Life Sci, Shijiazhuang 050016, Hebei, Peoples R China; [Feng, Feifei; Guang, Huijuan; Li, Zheng; Yu, Haining] Dalian Univ Technol, Sch Life Sci & Biotechnol, Dalian 116024, Liaoning, Peoples R China; [Wang, Yipeng] Chinese Acad Sci, Yantai Coastal Zone Reseach Inst, Yantai 264003, Shandong, Peoples R China; [Chi, Lianli] Shandong Univ, Natl Glycoengn Res Ctr, Jinan 250100, Shandong, Peoples R China
英文摘要Cathelicidins were initially characterized as a family of antimicrobial peptides. Now it is clear that they fulfill several immune functions in addition to their antimicrobial activity. In the current work, three cDNA sequences encoding pheasant cathelicidins were cloned from a constructed bone marrow cDNA library of Phasianus colchicus, using a nested-PCR-based cloning strategy. The three deduced mature antimicrobial peptides, Pc-CATH1, 2 and 3 are composed of 26, 32, and 29 amino acid residues, respectively. Unlike the mammalian cathelicidins that are highly divergent even within the same genus, Pc-CATHs are remarkably conserved with chicken fowlicidins with only a few of residues mutated according to the phylogenetic analysis result. Synthetic Pc-CATH1 exerted strong antimicrobial activity against most of bacteria and fungi tested, including the clinically isolated (IS) drug-resistant strains. Most MIC values against Gram-positive bacteria were in the range of 0.09-2.95 mu M in the presence of 100 mM NaCl. Pc-CATH1 displayed a negligible hemolytic activity against human erythrocytes, lysing 3.6% of erythrocytes at 3.15 mu M (10 mu g/ml), significantly higher than the corresponding MIC. Pc-CATH1 was stable in the human serum for up to 72 h, revealing its extraordinary serum stability. These specific features of Pc-CATH1 may make its applications much wider given the potency and breadth of the peptide's bacteriocidal capacity and its resistance towards serum and high-salt environments. (C) 2010 Elsevier Ltd. All rights reserved.
学科主题Immunology ; Zoology
公开日期2011-07-22
内容类型期刊论文
源URL[http://ir.yic.ac.cn/handle/133337/4874]  
专题烟台海岸带研究所_海岸带生物学与生物资源利用所重点实验室
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Wang, Yipeng,Lu, Zekuan,Feng, Feifei,et al. Molecular cloning and characterization of novel cathelicidin-derived myeloid antimicrobial peptide from Phasianus colchicus[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2011,35(3):314-322.
APA Wang, Yipeng.,Lu, Zekuan.,Feng, Feifei.,Zhu, Wei.,Guang, Huijuan.,...&Yu, Haining.(2011).Molecular cloning and characterization of novel cathelicidin-derived myeloid antimicrobial peptide from Phasianus colchicus.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,35(3),314-322.
MLA Wang, Yipeng,et al."Molecular cloning and characterization of novel cathelicidin-derived myeloid antimicrobial peptide from Phasianus colchicus".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 35.3(2011):314-322.
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