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Microbial Cell Factories

, 5:22

First Online: 20 June 2006Received: 27 April 2006Accepted: 20 June 2006

Abstract

Expressing proteins of interest as fusions to proteins of the bacterial envelope is a powerful technique with many biotechnological and medical applications. Autotransporters have recently emerged as a good tool for bacterial surface display. These proteins are composed of an N-terminal signal peptide, followed by a passenger domain and a translocator domain that mediates the outer membrane translocation of the passenger. The natural passenger domain of autotransporters can be replaced by heterologous proteins that become displayed at the bacterial surface by the translocator domain. The simplicity and versatility of this system has made it very attractive and it has been used to display functional enzymes, vaccine antigens as well as polypeptides libraries. The recent advances in the study of the translocation mechanism of autotransporters have raised several controversial issues with implications for their use as display systems. These issues include the requirement for the displayed polypeptides to remain in a translocation-competent state in the periplasm, the requirement for specific signal sequences and -autochaperone- domains, and the influence of the genetic background of the expression host strain. It is therefore important to better understand the mechanism of translocation of autotransporters in order to employ them to their full potential. This review will focus on the recent advances in the study of the translocation mechanism of autotransporters and describe practical considerations regarding their use for bacterial surface display.

AbbreviationsAIDA-IAdhesin involved in diffuse adherence

ATAutotransporter

CtxBCholera toxin B subunit

FACSFluorescence assisted cell sorting

OMPOuter membrane protein

SecGeneral secretion machinery

ScFvSingle chain antibody variable fragment

SPATEsSerine proteases autotransporters of Enterobacteriacae

TatTwin arginine translocation

TPSTwo-partner secretion

TUTranslocation Unit

Electronic supplementary materialThe online version of this article doi:10.1186-1475-2859-5-22 contains supplementary material, which is available to authorized users.

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Autor: Nancy Rutherford - Michael Mourez

Fuente: https://link.springer.com/







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