Studies of the human defensins have been hampered by the lack of a simple expression system allowing for rapid production of functional peptide forms. Here, we describe a Saccharomyces cerevisiae AH22 expression system that meets that condition. The 42 amino acid form of human beta-defensin-1 was expressed under the control of the ADH1 promoter. The optimum conditions for expression were determined and the stable maintenance of the pVT103L-hBD-1 chimeric vector in the yeast population was confirmed. Expressed hBD-1 was secreted into the medium (approximately 55 microg l(-1)) and purified using cation-exchange chromatography. Isolated defensin exhibited strong bactericidal effect on Escherichia coli ML-35p. We conclude that the expression system described here will be a useful tool where readily prepared and active forms of the human defensins are needed.

• MeSH
• antibakteriální látky biosyntéza   izolace a purifikace   farmakologie   MeSH
• beta-defensiny biosyntéza   chemie   genetika   farmakologie   MeSH
• Escherichia coli cytologie   účinky léků   MeSH
• genetické vektory genetika   MeSH
• lidé MeSH
• molekulární sekvence - údaje MeSH
• proliferace buněk účinky léků   MeSH
• rekombinantní proteiny biosyntéza   chemie   izolace a purifikace   farmakologie   MeSH
• Saccharomyces cerevisiae genetika   MeSH
• sekvence aminokyselin MeSH
• Check Tag
• lidé MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• antibakteriální látky MeSH
• beta-defensiny MeSH
• rekombinantní proteiny MeSH