摘要
Insect defensin A is an inducible antibacterial peptide of the fleshfly Phormia terranovae and has been recently characterized as a 40 residue basic peptide with six cysteines engaged in three intramolecular disulfide bridges. We report the expression of this peptide in Saccharomyces cerevisiae as a fusion protein carrying at its N-terminus leader sequences which are derived from the precursor of the yeast pheromone mating factor alpha (MF-alpha-1). These sequences allow the biologically active peptide to be secreted at high levels in a correctly processed form. Thus heterologous production of defensin A circumvents laborious purification of minute amounts of the peptide from its natural source. The insect defensin pro peptide can substitute for the MF-alpha-1 pro peptide, indicating that yeast can process an insect pro sequence.
- 出版日期1992-2