David Wickström

TL;DR: A stalled translocation intermediate of the autotransporter Hbp is used to identify components involved in insertion and translocation of the protein across the outer membrane and suggests a critical role for this general machinery in the translocation and insertion and assembly of outer-membrane proteins.

TL;DR: The data suggest that Hbp can fold in the periplasm but must retain a certain degree of flexibility and/or modest width to allow translocation across the outer membrane.

TL;DR: The bacterium Escherichia coli is the most widely used expression host for overexpression trials of membrane proteins, and recent studies have shown that it is feasible to engineer or select for E. coli strains with strongly improved membrane protein overextression characteristics.

TL;DR: This study suggests that several secretory and inner membrane proteins can use Sec translocon-independent pathways or have superior access to the remaining Sec translocons present in SecE-depleted cells.

TL;DR: The Escherichia coli AT Hemoglobin protease is engineered into a platform for the secretion and surface display of heterologous proteins, using the Mycobacterium tuberculosis vaccine target ESAT6 as a model protein, and the platform has potential with regard to the development of recombinant live vaccines.