[1].Novel Cathelicidins with Potent Antimicrobial, Biofilm Inhibitory, and Anti-inflammatory Activities from the Frog Fejervarya multistriata[J].Asian Herpetological Research,2017,8(3):199-212.[doi:10.16373/j.cnki.ahr.160067]
 Aili WANG,Yan CHEN,Haining YU*,et al.Novel Cathelicidins with Potent Antimicrobial, Biofilm Inhibitory, and Anti-inflammatory Activities from the Frog Fejervarya multistriata[J].Asian Herpetological Reserch(AHR),2017,8(3):199-212.[doi:10.16373/j.cnki.ahr.160067]

Novel Cathelicidins with Potent Antimicrobial, Biofilm Inhibitory, and Anti-inflammatory Activities from the Frog Fejervarya multistriata()

Asian Herpetological Research[ISSN:2095-0357/CN:51-1735/Q]



Novel Cathelicidins with Potent Antimicrobial, Biofilm Inhibitory, and Anti-inflammatory Activities from the Frog Fejervarya multistriata
Aili WANG1 Yan CHEN2 Haining YU3* Yipeng WANG2*
1 Weifang University of Science and Technology, Shouguang 262700, Shandong, China
2 Department of Pharmaceutical Sciences, College of Pharmaceutical Sciences, Soochow University, Suzhou 215123, Jiangsu, China
3 Department of Bioscience and Biotechnology, Dalian University of Technology, Dalian 116023, Liaoning, China
cathelicidin Fejervarya multistriata FM-CATHs antimicrobial peptide bacterial biofilm anti-inflammatory
Antimicrobial peptides (AMPs),?a class of gene-encoded peptides, are the first line of immune system to defense microbial invasions in multicellular organisms. Cathelicidins are an important family of AMPs that have been identified exclusively in vertebrates. However, up to now, cathelicidins from amphibians are poorly understood. In the present study, we reported the identification and characterization of two novel cathelicidins (FM-CATH1 and FM-CATH2) from the frog Fejervarya multistriata. The cDNA sequences encoding FM-CATHs were successfully cloned from the constructed lung cDNA library of F. multistriata. Both of the cDNA sequences encoding FM-CATHs are 447 bp in length, and the deduced mature peptides of FM-CATHs are composed of 34 residues. Structural analysis indicated that FM-CATH1 and FM-CATH2 mainly assume amphipathic alpha-helical conformations. Antimicrobial and bacterial killing kinetic analysis indicated that both FM-CATH1 and FM-CATH2 possess potent, broad-spectrum and rapid antimicrobial potency. And cytoplasmic membrane permeabilization analysis indicated that FM-CATH1 and FM-CATH2 kill bacteria by inducing the permeabilization of bacterial membrane. Besides direct antimicrobial activities, FM-CATHs also exhibited significant inhibitory effect on the formation of bacterial biofilms at low concentrations below 1×MIC. Furthermore, FM-CATH1 and FM-CATH2 exhibited potent anti-inflammatory activities by inhibiting LPS-induced transcription and production of pro-inflammatory cytokines TNF-α, IL-1β, and IL-6 in mouse peritoneal macrophages. Meanwhile, FM-CATHs showed relatively low cytotoxic activity against mammalian normal and tumor cell lines, and low hemolytic activity against human erythrocytes. In summary, the identification of FM-CATHs provides novel clues for our understanding of the roles of cathelicidins in amphibian immune systems. The potent antimicrobial, biofilm inhibitory, anti-inflammatory activities, and low cytotoxicity of FM-CATHs imply their great potential in novel antibiotics development.


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更新日期/Last Update: 2017-09-25