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Team:Paris/Addressing overview2
From 2009.igem.org
iGEM > Paris > Adressing > ClyA
Introduction
Bacterial pathogens display proteins on their surface that may interact with their hosts in order to mount successful infections. Although the primary function of the peptidoglycan is to provide a physical barrier for protection against both mechanical and osmotic stresses, it also serves as a scaffold to anchor external structures such as the outer cell membrane in Escherichia Coli. Over the past 20 years, it has become apparent that Gram-positive bacteria have evolved a variety of mechanism by which proteins are displayed on the cell surface (Tat and Sec transporter for example, cf the section "to the periplasm, export system" for more information about them). One of the major protein of the bacterial membrane is OmpA.
OmpA :
ClyA :
Pore-forming toxins (PFTs) are a class of potent virulence factors that convert from a soluble form to a membrane-integrated pore1. They exhibit their toxic effect either by destruction of themembrane permeability barrier or by delivery of toxic components through the pores.
Cytolysin A (ClyA, also known as HlyE), a PFT, is a cytolytic α-helical toxin responsible for the haemolytic phenotype of several Escherichia coli. (1)
Althought the toxic effect of Cly A we decided to use it to adress protein to the external membrane because ClyA contain the signal peptide required to be exported form the cytoplasm to the outer membrane.
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