Direct expression of antimicrobial peptides in an intact form by a translationally coupled two-cistron expression system Export

@article{citeulike:4301691, abstract = {We describe a novel prokaryotic expression system for the production of cationic antimicrobial peptides (AMPs). The method relies on a translationally coupled two-cistron system, in which the termination codon for the first cistron (which encodes the anionic polypeptide mIFc2, a derivative of human interferon-{gamma}) overlaps with the initiation codon for the second cistron (which encodes a cationic AMP) in the sequence of 5'-TAATG-3'. By forming an insoluble complex with the AMP upon translation, the mIFc2 protein efficiently neutralized the toxicity of the co-expressed cationic AMP and minimized the sensitivity of AMP to proteolytic degradation in a host. The AMPs were retrieved from the insoluble inclusion bodies without any chemical or enzymatic cleavage step by simple cation-exchange chromatography. With our system, [\~{}]100 mg of various AMPs (buforin IIb, parasin I, and pexiganan) were obtained from 1 L of Escherichia coli culture. Our expression system may represent a universal cost-effective solution for the mass production of intact AMPs in their natural forms. 10.1128/AEM.02753-08}, author = {Jang, Su A. and Sung, Bong H. and Cho, Ju H. and Kim, Sun C.}, citeulike-article-id = {4301691}, citeulike-linkout-0 = {http://dx.doi.org/10.1128/AEM.02753-08}, day = {10}, doi = {10.1128/AEM.02753-08}, journal = {Appl. Environ. Microbiol.}, keywords = {expression, gene, operon}, month = {April}, pages = {AEM.02753-08+}, posted-at = {2009-04-11 18:04:39}, priority = {2}, title = {Direct expression of antimicrobial peptides in an intact form by a translationally coupled two-cistron expression system}, url = {http://dx.doi.org/10.1128/AEM.02753-08}, year = {2009} }

TY - JOUR ID - citeulike:4301691 L3 - citeulike-article-id:4301691 N2 - We describe a novel prokaryotic expression system for the production of cationic antimicrobial peptides (AMPs). The method relies on a translationally coupled two-cistron system, in which the termination codon for the first cistron (which encodes the anionic polypeptide mIFc2, a derivative of human interferon-{gamma}) overlaps with the initiation codon for the second cistron (which encodes a cationic AMP) in the sequence of 5'-TAATG-3'. By forming an insoluble complex with the AMP upon translation, the mIFc2 protein efficiently neutralized the toxicity of the co-expressed cationic AMP and minimized the sensitivity of AMP to proteolytic degradation in a host. The AMPs were retrieved from the insoluble inclusion bodies without any chemical or enzymatic cleavage step by simple cation-exchange chromatography. With our system, [~]100 mg of various AMPs (buforin IIb, parasin I, and pexiganan) were obtained from 1 L of Escherichia coli culture. Our expression system may represent a universal cost-effective solution for the mass production of intact AMPs in their natural forms. 10.1128/AEM.02753-08 JF - Appl. Environ. Microbiol. TI - Direct expression of antimicrobial peptides in an intact form by a translationally coupled two-cistron expression system SP - AEM.02753-08 KW - expression KW - gene KW - operon AU - Jang, Su AU - Sung, Bong AU - Cho, Ju AU - Kim, Sun PY - 2009/04/10/ UR - http://dx.doi.org/10.1128/AEM.02753-08 ER -