Piers K L, Hancock R E
Department of Microbiology and Immunology, University of British Columbia, Vancouver, Canada.
Mol Microbiol. 1994 Jun;12(6):951-8. doi: 10.1111/j.1365-2958.1994.tb01083.x.
A cecropin/melittin hybrid peptide (CEME) produced by recombinant DNA procedures was tested for its ability to interact with the outer membrane of Pseudomonas aeruginosa and found to have identical biological properties to that of chemically synthesized CEME. CEME was shown to kill P. aeruginosa and permeabilize its outer membrane to lysozyme and 1-N-phenylnaphthlyamine, in some cases better than other antimicrobial agents and permeabilizers. CEME demonstrated a high-binding affinity to purified P. aeruginosa lipopolysaccharide (LPS) and LPS in whole-cell environments. These data provide information on the molecular mechanism of CEME antimicrobial activity and strongly suggest that it is taken up across the outer membrane by the self-promoted uptake pathway.
通过重组DNA程序产生的一种天蚕素/蜂毒素杂合肽（CEME），对其与铜绿假单胞菌外膜相互作用的能力进行了测试，发现其具有与化学合成的CEME相同的生物学特性。结果表明，CEME可杀死铜绿假单胞菌，并使其外膜对溶菌酶和1-N-苯基萘胺具有通透性，在某些情况下，其效果优于其他抗菌剂和通透剂。CEME在全细胞环境中对纯化的铜绿假单胞菌脂多糖（LPS）和LPS表现出高结合亲和力。这些数据提供了关于CEME抗菌活性分子机制的信息，并有力地表明它通过自促进摄取途径穿过外膜被摄取。
