| Autor: |
Allen-Vercoe, Emma, Toh, Michael C.W., Waddell, Barbara, Ho, Harmony, DeVinney, Rebekah |
| Předmět: |
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| Zdroj: |
FEMS Microbiology Letters; Feb2005, Vol. 243 Issue 2, p355-364, 10p |
| Abstrakt: |
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 TirΔ519–524 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. [Copyright &y& Elsevier] |
| Databáze: |
Complementary Index |
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