Study on Expression,Biological Stability and Anti-inflammatory Properties of a Novel Antimicrobial peptide Lacticin Q
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- 英文论文题名：Study on Expression,Biological Stability and Anti-inflammatory Properties of a Novel Antimicrobial peptide Lacticin Q
- 论文作者：Lulu Zhang ; Dayong Si ; Xubiao Wei ; Rijun Zhang
- 英文论文作者：Lulu Zhang ; Dayong Si ; Xubiao Wei ; Rijun Zhang ; Laboratory of Feed Biotechnology ; State Key Laboratory of Animal Nutrition ; College of Animal Science and Technology ; China Agricultural University
- 年：2016
- 作者机构：Laboratory of Feed Biotechnology,State Key Laboratory of Animal Nutrition,College of Animal Science and Technology,China Agricultural University;
- 英文论文关键词：antimicrobial peptide ; Lacticin Q ; fusion expression ; Pichia pastoris ; antibacterial activity ; stablity
- 会议召开时间：2016-11-04
- 会议录名称：中国畜牧兽医学会动物微生态学分会第五届第十二次全国学术研讨会论文集
- 语种：英文
- 分类号：S816
- 学会代码：ZGXJ
- 会议名称：中国畜牧兽医学会动物微生态学分会第五届第十二次全国学术研讨会
- 会议地点：中国山东青岛
- 主办单位：中国畜牧兽医学会动物微生态学分会
- 学会名称：中国畜牧兽医学会
- 页数：1
- 文件大小：65k
- 原文格式：O
- 会议级别：全国
摘要
The antimicrobial peptide Lacticin Q(LQ),which contains 53 amino acid residues,is a novel antimicrobial(AMPs) produced by Lactococcus lactis QU 5~([1]).LQ shows excellent thermostablity and acid-alkali tolerance and exhibits inhibitory activity against a wide range of pathogens~([1,2]).However,the low quantity of LQ produced by natural strains limited the further research and therapeutic application in feed industry.Recently,several biological systems have been developed in bacterial system for the high-production of AMPs~([3,4]).In our study,we efficiently expressed recomobinant LQ in Pichia pastoris(P.pastoris),and 32 mg pure LQ was obtained from fermentation liquid.The effects of temperature and pH on recombinant LQ was tested,and results showed that pH(from 3.0 to 8.0) and temperature(70,80,90 ℃) had a little effect on the biological activity of recombinant LQ.Another experiment was conducted to evaluate the effects of LQ on inflammatory response of mouse undergoing Staphylococcus aureus challenge.The results indicated that a low concentration of LQ(15 mg/mL) significantly reduced S.aureus-indaced inflammatory injury.Specifically,15 mg/mL LQ significantly decreased the decreased the expression of IL-1β,IL-6 and TNF-α(P < 0.05),which showed a direct activation of the inflammatory response that caused tissue destruction and a disease.In sum,this research not only supplied an effective approach for overproducing antibacterial peptide LQ,but paved the way for its further exploration on pharmaceutical potential and medical importance.
The antimicrobial peptide Lacticin Q(LQ),which contains 53 amino acid residues,is a novel antimicrobial(AMPs) produced by Lactococcus lactis QU 5~([1]).LQ shows excellent thermostablity and acid-alkali tolerance and exhibits inhibitory activity against a wide range of pathogens~([1,2]).However,the low quantity of LQ produced by natural strains limited the further research and therapeutic application in feed industry.Recently,several biological systems have been developed in bacterial system for the high-production of AMPs~([3,4]).In our study,we efficiently expressed recomobinant LQ in Pichia pastoris(P.pastoris),and 32 mg pure LQ was obtained from fermentation liquid.The effects of temperature and pH on recombinant LQ was tested,and results showed that pH(from 3.0 to 8.0) and temperature(70,80,90 ℃) had a little effect on the biological activity of recombinant LQ.Another experiment was conducted to evaluate the effects of LQ on inflammatory response of mouse undergoing Staphylococcus aureus challenge.The results indicated that a low concentration of LQ(15 mg/mL) significantly reduced S.aureus-indaced inflammatory injury.Specifically,15 mg/mL LQ significantly decreased the decreased the expression of IL-1β,IL-6 and TNF-α(P < 0.05),which showed a direct activation of the inflammatory response that caused tissue destruction and a disease.In sum,this research not only supplied an effective approach for overproducing antibacterial peptide LQ,but paved the way for its further exploration on pharmaceutical potential and medical importance.
The antimicrobial peptide Lacticin Q(LQ),which contains 53 amino acid residues,is a novel antimicrobial(AMPs) produced by Lactococcus lactis QU 5~([1]).LQ shows excellent thermostablity and acid-alkali tolerance and exhibits inhibitory activity against a wide range of pathogens~([1,2]).However,the low quantity of LQ produced by natural strains limited the further research and therapeutic application in feed industry.Recently,several biological systems have been developed in bacterial system for the high-production of AMPs~([3,4]).In our study,we efficiently expressed recomobinant LQ in Pichia pastoris(P.pastoris),and 32 mg pure LQ was obtained from fermentation liquid.The effects of temperature and pH on recombinant LQ was tested,and results showed that pH(from 3.0 to 8.0) and temperature(70,80,90 ℃) had a little effect on the biological activity of recombinant LQ.Another experiment was conducted to evaluate the effects of LQ on inflammatory response of mouse undergoing Staphylococcus aureus challenge.The results indicated that a low concentration of LQ(15 mg/mL) significantly reduced S.aureus-indaced inflammatory injury.Specifically,15 mg/mL LQ significantly decreased the decreased the expression of IL-1β,IL-6 and TNF-α(P < 0.05),which showed a direct activation of the inflammatory response that caused tissue destruction and a disease.In sum,this research not only supplied an effective approach for overproducing antibacterial peptide LQ,but paved the way for its further exploration on pharmaceutical potential and medical importance.
引文
[1]Fujita,K.,S.Ichimasa,T.Zendo,et al.Structural analysis and characterization of lacticin Q,a novel bacteriocin belonging to a new family of unmodified bacteriocins gram-positive bacteria.Applied and Environmental Microbiology.2007;73(9):2871-2877.
[2]Svetoch,E.A.,B.V.Eruslanov,V.V.Perelygin,et al.Diverse antimicrobial killing by Enterococcus faecium E 50-52bacteriocin.Journal of Agricultural and Food Chemistry.2008;56(6):1942-1948.
[3]Li,B.C.,S.Q.Zhang,W.B.Dan,et al.Expression in Escherichia coli and purification of bioactive antibacterial peptide ABP-CM4 from the Chinese silk worm,Bombyx mori.Biotechnology Letters.2007;29(7):1031-1036.
[4]Moon,G-S.,Y.-R.Pyun,W.J.Kim,et al.Expression and purification of a fusion-typed pediocin PA-1 in Escherichia coli and recovery of biologically active pediocin PA-1.International Journal of Food Microbiology.2006;108(1):136-140.
[2]Svetoch,E.A.,B.V.Eruslanov,V.V.Perelygin,et al.Diverse antimicrobial killing by Enterococcus faecium E 50-52bacteriocin.Journal of Agricultural and Food Chemistry.2008;56(6):1942-1948.
[3]Li,B.C.,S.Q.Zhang,W.B.Dan,et al.Expression in Escherichia coli and purification of bioactive antibacterial peptide ABP-CM4 from the Chinese silk worm,Bombyx mori.Biotechnology Letters.2007;29(7):1031-1036.
[4]Moon,G-S.,Y.-R.Pyun,W.J.Kim,et al.Expression and purification of a fusion-typed pediocin PA-1 in Escherichia coli and recovery of biologically active pediocin PA-1.International Journal of Food Microbiology.2006;108(1):136-140.