Design and recombination expression of a novel plectasin-derived peptide MP1106 and its properties against Staphylococcus aureus

Verfasser / Beitragende:
[Xintao Cao, Yong Zhang, Ruoyu Mao, Da Teng, Xiumin Wang, Jianhua Wang]
Ort, Verlag, Jahr:
2015
Enthalten in:
Applied Microbiology and Biotechnology, 99/6(2015-03-01), 2649-2662
Format:
Artikel (online)
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024 7 0 |a 10.1007/s00253-014-6077-9  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00253-014-6077-9 
245 0 0 |a Design and recombination expression of a novel plectasin-derived peptide MP1106 and its properties against Staphylococcus aureus  |h [Elektronische Daten]  |c [Xintao Cao, Yong Zhang, Ruoyu Mao, Da Teng, Xiumin Wang, Jianhua Wang] 
520 3 |a A novel antimicrobial peptide MP1106 was designed based on the parental peptide plectasin with four mutational sites and a high level of expression in Pichia pastoris X-33 via the pPICZαA plasmid was achieved. The concentration of total secreted protein in the fermented supernatant was 2.134g/l (29°C), and the concentration of recombinant MP1106 (rMP1106) reached 1,808mg/l after a 120-h induction in a 5-l fermentor. The rMP1106 was purified using a cation-exchange column, and the yield was 831mg/l with 94.68% purity. The sample exhibited a narrow spectrum against some Gram-positive bacteria and strong antimicrobial activity against Staphylococcus aureus at low minimal inhibitory concentrations (MICs) of 0.014, 1.8, 0.45, and 0.91μM to S. aureus strains ATCC 25923, 29213, 6538, and 43300, respectively. Meanwhile, rMP1106 showed potent activity (0.03-1.8μM) against 20 clinical isolates of methicillin-resistant S. aureus (MRSA). In addition, rMP1106 exhibited a broad range of thermostability from 20 to 100°C. The higher antimicrobial activity of rMP1106 was maintained in neutral and alkaline environments (pH 6, 8, and 10), and its activity was slightly reduced in acidic environments (pH 2 and 4). The rMP1106 was resistant to the digestion of pepsin, snailase, and proteinase K and was sensitive to trypsin. It exhibited hemolytic activity of only 1.16% at a concentration of 512μg/ml and remained stable in human serum at 37°C for 24h. Furthermore, the activity of rMP1106 was minorly affected by 10mM dithiothreitol and 20% dimethylsulfoxide. Our results indicate that MP1106 can be produced on a large scale and has potential as a therapeutic drug against S. aureus. 
540 |a Springer-Verlag Berlin Heidelberg, 2014 
690 7 |a MP1106  |2 nationallicence 
690 7 |a Antimicrobial peptide  |2 nationallicence 
690 7 |a Pichia pastoris  |2 nationallicence 
690 7 |a Stability  |2 nationallicence 
690 7 |a Staphylococcus aureus  |2 nationallicence 
700 1 |a Cao  |D Xintao  |u Key Laboratory of Feed Biotechnology, Ministry of Agriculture, 100081, Beijing, China  |4 aut 
700 1 |a Zhang  |D Yong  |u Key Laboratory of Feed Biotechnology, Ministry of Agriculture, 100081, Beijing, China  |4 aut 
700 1 |a Mao  |D Ruoyu  |u Key Laboratory of Feed Biotechnology, Ministry of Agriculture, 100081, Beijing, China  |4 aut 
700 1 |a Teng  |D Da  |u Key Laboratory of Feed Biotechnology, Ministry of Agriculture, 100081, Beijing, China  |4 aut 
700 1 |a Wang  |D Xiumin  |u Key Laboratory of Feed Biotechnology, Ministry of Agriculture, 100081, Beijing, China  |4 aut 
700 1 |a Wang  |D Jianhua  |u Key Laboratory of Feed Biotechnology, Ministry of Agriculture, 100081, Beijing, China  |4 aut 
773 0 |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/6(2015-03-01), 2649-2662  |x 0175-7598  |q 99:6<2649  |1 2015  |2 99  |o 253 
856 4 0 |u https://doi.org/10.1007/s00253-014-6077-9  |q text/html  |z Onlinezugriff via DOI 
898 |a BK010053  |b XK010053  |c XK010000 
900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a research-article  |2 jats 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-springer 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1007/s00253-014-6077-9  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Cao  |D Xintao  |u Key Laboratory of Feed Biotechnology, Ministry of Agriculture, 100081, Beijing, China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Zhang  |D Yong  |u Key Laboratory of Feed Biotechnology, Ministry of Agriculture, 100081, Beijing, China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Mao  |D Ruoyu  |u Key Laboratory of Feed Biotechnology, Ministry of Agriculture, 100081, Beijing, China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Teng  |D Da  |u Key Laboratory of Feed Biotechnology, Ministry of Agriculture, 100081, Beijing, China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Wang  |D Xiumin  |u Key Laboratory of Feed Biotechnology, Ministry of Agriculture, 100081, Beijing, China  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Wang  |D Jianhua  |u Key Laboratory of Feed Biotechnology, Ministry of Agriculture, 100081, Beijing, China  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t Applied Microbiology and Biotechnology  |d Springer Berlin Heidelberg  |g 99/6(2015-03-01), 2649-2662  |x 0175-7598  |q 99:6<2649  |1 2015  |2 99  |o 253