Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
9121867 | FEMS Microbiology Letters | 2005 | 10 Pages |
Abstract
The type III secreted protein Tir from Enterohemorrhagic Escherichia coli (EHEC O157:H7) plays a central role in adherence and pedestal formation during infection. Little is known about how Tir domains outside of the amino-terminus contribute to efficient Tir secretion and translocation. We found a 6 amino acid (519-524) carboxy-terminal region which was required for efficient Tir secretion and translocation. Interestingly, EHEC O157:H7 TirÎ519-524 was efficiently secreted when expressed in the related pathogen enteropathogenic E. coli. These data suggest that this region may play a role in maintaining EHEC O157:H7 Tir in a secretion-competent conformation.
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Authors
Emma Allen-Vercoe, Michael C.W. Toh, Barbara Waddell, Harmony Ho, Rebekah DeVinney,