IcsA autotransporter passenger promotes increased fusion protein expression on the cell surface.

ABSTRACT:

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 localisation and folding of TEM-1 β-lactamase (Bla) and maltose binding protein (MalE or MBP) fused to either full length Shigella flexneri IcsA (IcsA) autotransporter or to the β domain alone (IcsAβ) to determine the contribution of the native IcsA α domain in presenting the fusion proteins on the surface of E. coli K-12 UT5600 (ΔompT).

Results

Expression of IcsA-Bla was greater than Ic

SUBMITTER: Lum M 

PROVIDER: S-EPMC3298707 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature