Novel cathelicidin-derived antimicrobial peptides from Equus asinus
Lu ZK1; Wang YP2,3; Zhai L1; Che QL3; Wang H1; Du SY1; Wang D1; Feng FF1,2; Liu JZ1; Lai R*3; Yu HN*1,2; rlai@mail.kiz.ac.cn; yuhaining@dlut.edu.cn
2010
发表期刊FEBS JOURNAL
ISSN1742-464X
卷号277期号:10页码:2329-2339
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摘要In the present study, EA-CATH1 and EA-CATH2 were identified from a constructed lung cDNA library of donkey (Equus asinus) as members of cathelicidin-derived antimicrobial peptides, using a nested PCR-based cloning strategy. Composed of 25 and 26 residues, respectively, EA-CATH1 and EA-CATH2 are smaller than most other cathelicidins and have no sequence homology to other cathelicidins identified to date. Chemically synthesized EA-CATH1 exerted potent antimicrobial activity against most of the 32 strains of bacteria and fungi tested, especially the clinically isolated drug-resistant strains, and minimal inhibitory concentration values against Gram-positive bacteria were mostly in the range of 0.3-2.4 mu g center dot mL-1. EA-CATH1 showed an extraordinary serum stability and no haemolytic activity against human erythrocytes in a dose up to 20 mu g center dot mL-1. CD spectra showed that EA-CATH1 mainly adopts an alpha-helical conformation in a 50% trifluoroethanol/water solution, but a random coil in aqueous solution. Scanning electron microscope observations of Staphylococcus aureus (ATCC2592) treated with EA-CATH1 demonstrated that EA-CATH could cause rapid disruption of the bacterial membrane, and in turn lead to cell lysis. This might explain the much faster killing kinetics of EA-CATH1 than conventional antibiotics revealed by killing kinetics data. In the presence of CaCl(2), EA-CATH1 exerted haemagglutination activity, which might potentiate an inhibition against the bacterial polyprotein interaction with the host erythrocyte surface, thereby possibly restricting bacterial colonization and spread.
关键词Cathelicidin Equus Asinus Function Gene Cloning Peptide Identification
资助者This work was supported by grants from the Chinese National Natural Science Foundation (30900240). ; This work was supported by grants from the Chinese National Natural Science Foundation (30900240). ; This work was supported by grants from the Chinese National Natural Science Foundation (30900240). ; This work was supported by grants from the Chinese National Natural Science Foundation (30900240).
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语种英语
资助者This work was supported by grants from the Chinese National Natural Science Foundation (30900240). ; This work was supported by grants from the Chinese National Natural Science Foundation (30900240). ; This work was supported by grants from the Chinese National Natural Science Foundation (30900240). ; This work was supported by grants from the Chinese National Natural Science Foundation (30900240).
文献类型期刊论文
条目标识符http://ir.kiz.ac.cn/handle/152453/2573
专题科研部门_天然药物功能蛋白质学科组(赖仞)
科研部门_动物模型与人类重大疾病机理重点实验室
通讯作者rlai@mail.kiz.ac.cn; yuhaining@dlut.edu.cn
作者单位1.College of Life Sciences, Hebei Normal University, Shijiazhuang, China
2.School of Life Science and Biotechnology, Dalian University of Technology, China
3.Key Laboratory of Animal Models and Human Disease Mechanisms, Kunming Institute of Zoology, Chinese Academy of Sciences, Kunming, Yunnan, China
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Lu ZK,Wang YP,Zhai L,et al. Novel cathelicidin-derived antimicrobial peptides from Equus asinus[J]. FEBS JOURNAL,2010,277(10):2329-2339.
APA Lu ZK.,Wang YP.,Zhai L.,Che QL.,Wang H.,...&yuhaining@dlut.edu.cn.(2010).Novel cathelicidin-derived antimicrobial peptides from Equus asinus.FEBS JOURNAL,277(10),2329-2339.
MLA Lu ZK,et al."Novel cathelicidin-derived antimicrobial peptides from Equus asinus".FEBS JOURNAL 277.10(2010):2329-2339.
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