IcsA autotransporter passenger promotes increased fusion protein expression on the cell surface
نویسندگان
چکیده
منابع مشابه
IcsA autotransporter passenger promotes increased fusion protein expression on the cell surface
BACKGROUND Autotransporters are attractive cell surface display vehicles as they lack complex adaptor proteins necessary for protein export. Recent reports have suggested that the native effector domain (α domain) and translocation domain (β domain) interact with each other to drive translocation of the effector domain to the outer membrane. In this report we compared the expression, surface lo...
متن کاملInfluence of recombinant passenger properties and process conditions on surface expression using the AIDA-I autotransporter
Surface expression has attracted much recent interest, and it has been suggested for a variety of applications. Two such applications are whole-cell biocatalysis and the creation of live vaccines. For successful implementation of these applications there is a need for flexible surface expression systems that can yield a high level of expression with a variety of recombinant fusion proteins. The...
متن کاملContribution of the periplasmic chaperone Skp to efficient presentation of the autotransporter IcsA on the surface of Shigella flexneri.
IcsA is an outer membrane protein in the autotransporter family that is required for Shigella flexneri pathogenesis. Following its secretion through the Sec translocon, IcsA is incorporated into the outer membrane in a process that depends on YaeT, a component of an outer membrane beta-barrel insertion machinery. We investigated the role of the periplasmic chaperone Skp in IcsA maturation. Skp ...
متن کاملAutodisplay: functional display of active beta-lactamase on the surface of Escherichia coli by the AIDA-I autotransporter.
Members of the protein family of immunoglobulin A1 protease-like autotransporters comprise multidomain precursors consisting of a C-terminal autotransporter domain that promotes the translocation of N-terminally attached passenger domains across the cell envelopes of gram-negative bacteria. Several autotransporter domains have recently been shown to efficiently promote the export of heterologou...
متن کاملCrystal structure of the autochaperone region from the Shigella flexneri autotransporter IcsA.
The IcsA (intracellular spread gene A) autotransporter from Shigella flexneri is a key virulence factor. We identified a stable fragment comprising residues 591 to 758, which corresponds to the autochaperone region of the IcsA passenger domain. We showed that thermal unfolding of the autochaperone region is reversible and determined its crystal structure at 2.0-Å resolution.
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ژورنال
عنوان ژورنال: Microbial Cell Factories
سال: 2012
ISSN: 1475-2859
DOI: 10.1186/1475-2859-11-20