Human Lysozyme Secretion Increased by Alpha-factor Pro-sequence in<i>Pichia pastoris</i>

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  • Human Lysozyme Secretion Increased by Alpha-factor Pro-sequence in Pichia pastoris.
  • Human lysozyme secretion increased by α-factor pro-sequence in Pichia pastoris

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  To get high level secretion of human lysozyme in Pichia pastoris, the following three signal sequences and one prepro sequence were evaluated: chicken lysozyme signal peptide, leucine-rich artificial signal peptide, Saccharomyces invertase signal peptide, and Saccharomyces prepro sequence of alpha factor (MF-α Prepro).<br>   Transformants harboring a lysozyme gene with MF-α Prepro secreted 20-fold more lysozyme than those harboring the lysozyme gene with any one of the other three signal sequences. Three mutant leader sequences derived from MF-α Prepro were constructed to discover the function of the pro region. The secretion was dramatically decreased by eliminating the pro region of MF-α Prepro. In contrast, MF-α Prepro with the EAEAEA sequence directed the secretion of an equivalent level of lysozyme having the extra amino acids (EAEAEA) in its N-terminus.<br>   For the effective secretion of native human lysozyme, MF-α Prepro without any spacer sequences was most suitable. The secreted protein by MF-α Prepro construct was identical with the authentic human lysozyme, judging from N-terminal amino acid sequencing and molecular mass spectrometric and crystallographic analysis.<br>

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