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J. Biol. Chem., Vol. 276, Issue 7, 4772-4780, February 16, 2001
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From the Bacterial invasion, like the process of
phagocytosis, involves extensive and localized protrusion of the host
cell plasma membrane. To examine the molecular mechanisms of the
membrane remodeling that accompanies bacterial invasion,
soluble NSF attachment protein
receptor (SNARE)-mediated membrane traffic was studied in
cultured cells during infection by Salmonella typhimurium. A green fluorescent protein-tagged chimera of VAMP3, a SNARE
characteristic of recycling endosomes, was found to accumulate at sites
of Salmonella invasion. To analyze the possible role of
SNARE-mediated membrane traffic in bacterial infection, invasion was
measured in cells expressing a dominant-negative form of
N-ethylmaleimide-sensitive factor (NSF), an essential regulator of membrane fusion.
Inhibition of NSF activity did not affect cellular invasion by S. typhimurium nor the associated membrane remodeling. By contrast,
Fc
Requirement for N-Ethylmaleimide-sensitive Factor
Activity at Different Stages of Bacterial Invasion and
Phagocytosis*
§,,,
**,,§§, and¶¶
Cell Biology Programme, Research Institute,
The Hospital for Sick Children, Toronto, Ontario M5G 1X8, the
Department of Biochemistry, University of Toronto,
Toronto, Ontario, Canada M5S1A8, the ¶ Department of
Medicine, University of Pennsylvania School of Medicine and
Biotechnology Laboratory, Philadelphia,
Pennsylvania 19104-4283, and the Biotechnology Laboratory,
University of British Columbia, Vancouver, British Columbia,
V6T1Z3 Canada
receptor-mediated phagocytosis was greatly reduced in the
presence of the mutant NSF. Most important, dominant-negative NSF
significantly impaired the fusion of Salmonella-containing
vacuoles with endomembranes. These observations indicate that the
membrane protrusions elicited by Salmonella invasion,
unlike those involved in phagocytosis, occur via an NSF-independent
mechanism, whereas maturation of Salmonella-containing
vacuoles is NSF-dependent.
*
This work was supported in part by the Arthritis Society of
Canada, The Sanatorium Foundation, and the Canadian Institutes of
Health Research.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Senior Scientist of the Canadian Institutes of Health Research
and a Howard Hughes International Investigator.
§§
International Scholar of the Howard Hughes Medical Institute, a
recipient of a Canadian Institutes of Health Research Distinguished Scientist award, and the current holder of the Pitblado Chair in Cell Biology.
¶¶
Recipient of a Canadian Institutes of Health Research
Scientist award. To whom correspondence should be addressed: Cell
Biology Programme, Hospital for Sick Children, 555 University Avenue, Toronto, Ontario M5G 1X8, Canada. E-mail:
wtrimble@sickkids.on.ca.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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