Keywords

Secretion Process, Signal Peptide, Protein Secretion, Exogenous Protein, Secreted Protein, Cytoplasm, Interaction, Total Protein, Physical Technology, Culture Medium

Abstract

At present, most of the expression vectors used in microbial genetic engineering direct the expression of target genes in the host’s cytoplasm. Although the yield of foreign proteins can reach more than 50% of the total bacterial protein, there are also many shortcomings: ( 1) Foreign proteins expressed at high levels are prone to sedimentation and aggregation, and are difficult to refold into the correct conformation, making it difficult to obtain functional products; (2) The product purification process is complex; (3) It has toxic effects on the host, causing the expression system to fail. Stable; (4) Foreign proteins are easily degraded by intracellular proteases. This greatly limits the application of microbial genetic engineering. If the exogenous protein expressed in the cytoplasm can be secreted out of the cell, various disadvantages caused by high protein expression can be corrected. In-depth research on protein localization in E.coli has been carried out in the past decade. The proteins of E.coli are initially synthesized in the cytoplasm and are localized in the membrane or periplasm through secretion. For example, outer membrane protein A (OmpA) is first synthesized in the cytoplasm as a precursor, and then crosses the inner membrane with the help of a signal peptide. During the secretion process, the signal peptide is cleaved into a mature protein that is localized in the outer membrane. Now many authors use the signal peptide sequence of E.coli secreted protein to fuse with the target gene to secrete foreign proteins out of the cytoplasm. For example, the signal peptide of alkaline phosphatase (phoA) is used to secrete human alpha interferon, which improves the stability and yield of the product, and the product can be obtained through simple physical techniques. E.coli hemolysin is secreted into the culture medium across the cell membrane through a special secretion mechanism. An attempt has been made to use this system to construct an expression vector. This article reviews the research on E.coli in recent years from the aspects of the role of signal peptide, the influence of mature proteins on secretion, the role of the host in secretion, the secretion of E.coli hemolysin and the secretion of foreign proteins in E.coli. Progress in protein secretion

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Original research done by Wu Weixing, Ma Xiankai

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