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Chlamydomonas reinhardtii-derived mytichitin-CB/hispidalin chimera efficiently inhibits the growth of bacteria by disrupting their membrane integrity

文献类型: 外文期刊

作者: Wang, Hui 1 ; Feng, Ying 1 ; Hadiatullah, Hadiatullah 1 ; Fan, Zhen-Chuan 1 ;

作者机构: 1.Inst Hlth Biotechnol, State Key Lab Food Nutr & Safety, Tianjin 300457, Peoples R China

2.Inner Mongolia Acad Agr & Anim Husb Sci, Hohhot 010031, Inner Mongolia, Peoples R China

3.Tianjin Econ & Technol Dev Area Tianjin Univ Sci &, Rm 334,Yifu Bldg 9 13St, Tianjin 300457, Peoples R China

关键词: Mytichitin-CB; Hispidalin; Antimicrobial peptide; Chlamydomonas reinhardtii

期刊名称:PROCESS BIOCHEMISTRY ( 影响因子:4.4; 五年影响因子:4.2 )

ISSN: 1359-5113

年卷期: 2023 年 130 卷

页码:

收录情况: SCI

摘要: The antimicrobial peptides Mytichitin-CB and Hispidalin were isolated from Mytilus coruscus and Benincasa hispida, respectively. Our previous studies showed that Mytichitin-CB, when expressed in Chlamydomonas reinhardtii, inhibits the bacterial growth with moderate efficiency. Naturally isolated or Pichia pastoris-expressed Hispidalin also exerts moderate efficiency for inhibiting the growth of bacteria. Here, we expressed a chimeric peptide composed of Mytichitin-CB and Hispidalin that we named as MCH in C. reinhardtii. MCH was stably expressed and its yield accounted for 0.18% of total soluble proteins of the host cells. C. reinhardtii-derived MCH inhibited the growth of both Gram-positive and Gram-negative bacteria by disrupting their cell membrane integrity. Its minimal inhibitory concentration (MIC) were ranged between 20 and 40 mu g/mL, demonstrating that MCH is more potent for inhibiting the bacterial growth than individual microalgae-expressed Mytichitin-CB and yeast-expressed Hispidalin. Of more importance, MCH was temperature- and pH-tolerant, protease-resistant and exhibited low hemolytic activity against rat erythrocytes and low cytotoxicity to human embryonic kidney 293 (HEK 293) and Madin-Darby bovine kidney (MDBK) cells. Therefore, we conclude that C. reinhardtii-derived chimeric peptide MCH has a great potential for being developed to replace traditional antibiotics in the future.

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