A specific antimicrobial protein CAP-1 from Pseudomonas sp isolated from the jellyfish Cyanea capillata

A specific antimicrobial protein CAP-1 from Pseudomonas sp isolated from the jellyfish Cyanea capillata
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从水母 Cyanea capillata 中分离出的假单胞菌的特异性抗菌蛋白 CAP-1

DOI:
10.1016/j.ijbiomac.2015.10.056
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发表时间:
2016
影响因子:
8.2
通讯作者:
Zhang Liming
Zhang Liming
中科院分区:
化学1区
文献类型:
--
作者:
Yin Manman;Liu Dan;Xu Feng;Xiao Liang;Wang Qianqian;Wang Beilei;Chang Yinlong;Zheng Jiemin;Tao Xia;Liu Guoyan;Zhang Liming

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从毛藻水母中分离出一株细菌CMF-2,其培养上清液具有显著的抑菌活性。菌株CMF-2经鉴定为假单胞菌。基于形态学、生化和生理特征以及16S rRNA序列分析。本研究通过硫酸铵沉淀和凝胶过滤层析从CMF-2培养物中分离出抗菌蛋白CAP-1。根据十二烷基硫酸钠-聚丙烯酰胺凝胶电泳(SDS-PAGE)结果,一条主谱带显示该抗菌蛋白分子量约为15 kDa,经MALDI-TOF-MS分析和Mascot搜索鉴定为假想蛋白。CAP-1对金黄色葡萄球菌、大肠杆菌、枯草芽孢杆菌和白色念珠菌等指示菌和真菌,特别是对创伤弧菌、溶藻弧菌、副溶血性弧菌、霍乱弧菌和鳗弧菌等海洋微生物具有较广的抗菌谱,但对肿瘤细胞和正常人体细胞影响不大。CAP-1蛋白在较宽的温度(20-80℃)和pH(2-10)条件下保持稳定的抗菌活性。这些结果表明,CAP-1可能具有非细胞毒性的特异性抗菌功能。
A bacterium strain, designated as CMF-2, was isolated from the jellyfishCyanea capillataand its culture supernatant exhibited a significant antimicrobial activity. The strain CMF-2 was identified asPseudomonassp. based on the morphological, biochemical and physiological characteristics as well as 16S rRNA sequence analysis. In this study, an antimicrobial protein, named as CAP-1, was isolated from the culture of CMF-2 through ammonium sulfate precipitation and gel filtration chromatography. According to the result of sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), a major band indicated that the antimicrobial protein had a molecular mass of about 15 kDa, and it was identified as a hypothetical protein by MALDI-TOF-MS analysis and Mascot searching. CAP-1 displayed a broad antimicrobial spectrum against the indicator bacteria and fungus, includingStaphylococcus aureus,Escherichia coli,Bacillus subtilisandCandida albicans, especially some marine-derived microorganisms such asVibrio vulnificus,Vibrio alginolyticus,Vibrio parahaemolyticus,Vibrio cholera, andVibrio anguillarum, but showed little impact on tumor cells and normal human cells. The protein CAP-1 remained a stable antimicrobial activity in a wide range of temperature (20–80 °C) and pH (2–10) conditions. These results suggested that CAP-1 might have a specific antimicrobial function not due to cytotoxicity.