TY - JOUR
T1 - Structural Microengineers
T2 - Pathogenic Escherichia coli Redesigns the Actin Cytoskeleton in Host Cells
AU - Sal-Man, Neta
AU - Biemans-Oldehinkel, Esther
AU - Finlay, B. Brett
N1 - Funding Information:
We thank W. Deng and other members of the Finlay lab for critical reading of this manuscript and F. Ness for assistance in figure preparation. This work was supported by operating grants to B.B.F. from the Canadian Institutes of Health Research, the Howard Hughes Medical Institute (HHMI), the Canadian Crohn's and Colitis Foundation, and Genome Canada. B.B.F. is an HHMI International Research Scholar and the University of British Columbia Peter Wall Distinguished Professor. N.S. is supported by Rothschild and MSFHR fellowships. E.B.O. is supported by a MSFHR fellowship.
PY - 2009/1/14
Y1 - 2009/1/14
N2 - Several virulent bacteria have the ability to manipulate the host cell actin cytoskeleton as part of their pathogenic strategy. These pathogens subvert the host cell actin polymerization machinery for various purposes including motility within host cells, cell-to-cell spread, and to prevent phagocytic engulfment by professional phagocytes. In contrast to intracellular pathogens, pathogenic Escherichia coli (including both enterohemorrhagic and enteropathogenic E. coli) subvert actin polymerization from an extracellular position to facilitate adherence. This review summarizes recent data on the mechanisms by which pathogenic E. coli hijack members of the Wiskott-Aldrich syndrome protein family to manipulate actin polymerization within host cells, including the novel, and surprisingly simple, mechanism recently revealed for the EspFu effector.
AB - Several virulent bacteria have the ability to manipulate the host cell actin cytoskeleton as part of their pathogenic strategy. These pathogens subvert the host cell actin polymerization machinery for various purposes including motility within host cells, cell-to-cell spread, and to prevent phagocytic engulfment by professional phagocytes. In contrast to intracellular pathogens, pathogenic Escherichia coli (including both enterohemorrhagic and enteropathogenic E. coli) subvert actin polymerization from an extracellular position to facilitate adherence. This review summarizes recent data on the mechanisms by which pathogenic E. coli hijack members of the Wiskott-Aldrich syndrome protein family to manipulate actin polymerization within host cells, including the novel, and surprisingly simple, mechanism recently revealed for the EspFu effector.
KW - MICROBIO
KW - PROTEINS
KW - SIGNALING
UR - http://www.scopus.com/inward/record.url?scp=58149180090&partnerID=8YFLogxK
U2 - 10.1016/j.str.2008.12.001
DO - 10.1016/j.str.2008.12.001
M3 - Short survey
AN - SCOPUS:58149180090
SN - 0969-2126
VL - 17
SP - 15
EP - 19
JO - Structure
JF - Structure
IS - 1
ER -