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Cutting Edge |
B Pathway1
* Epithelial Pathobiology Unit, Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, GA 30322;
Department of Biological Chemistry, University of Michigan, Ann Arbor, MI 48109; and
Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390
Secreted prokaryotic effector proteins have evolved to modulate
the cellular functions of specific eukaryotic hosts. Generally, these
proteins are considered virulence factors that facilitate parasitism.
However, in certain plant and insect eukaryotic/prokaryotic
relationships, effector proteins are involved in the establishment of
commensal or symbiotic interactions. In this study, we report that the
AvrA protein from Salmonella typhimurium, a common
enteropathogen of humans, is an effector molecule that inhibits
activation of the key proinflammatory NF-
B transcription factor and
augments apoptosis in human epithelial cells. This activity is
similar but mechanistically distinct from that described for YopJ, an
AvrA homolog expressed by the bacterial pathogen
Yersinia. We suggest that AvrA may limit virulence in
vertebrates in a manner analogous to avirulence factors in plants, and
as such, is the first bacterial effector from a mammalian pathogen that
has been ascribed such a function.
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