Influence of a-Factor over the expression of hrIDS in Pichia pastoris: Literature review and computational analysis. In searching of alternatives to get the efficient secretions of the recombinant enzyme Iduronate Sulfatase (IDSh) in Pichia pastoris, we made a systematic review of the literature so that we could compile information to relate the expression level of human heterologous proteins, with secretion signal, and the characteristics of the molecules. 349 publications were found of which only 7 (2%) reported the expression of proteins that met find inclusion criteria. With the information obtained in these articles, we made a hypothesis test using the data compiled as samples and a qualitative analysis of the information. It was found that replacement of native secretion signal by a-Factor as leader peptide increases the level of expression of human heterologous proteins in P. pastoris (p=0.053). Moreover, the elimination of native signal peptide in the protein cDNA is 125 indispensable for the function of a-Factor in the secretion of recombinant proteins and for to increase the expression level. In the construct, GS115/pPIC9-IDS were simultaneously founded two sequences in the signal peptide, the native and the a-Factor. However, the activity found ~30 mmol/h mg of protein raises the question of a possible conflict between the two recognition sites. This may be the cause given the similarity in the hidrophobicity of those two sites.
keywords:
systematic review, signal peptide, protein expression, Pichia pastoris