Journal
JOURNAL OF MOLECULAR BIOLOGY
Volume 384, Issue 2, Pages 465-477Publisher
ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2008.09.051
Keywords
type III secretion; virulence; cell cycle; Cif; crystallography
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Funding
- NIAID NIH HHS [R01 AI052182-04, R01 AI052182-03, R01 AI052182-05, R01 AI052182] Funding Source: Medline
- NIBIB NIH HHS [P30 EB009998] Funding Source: Medline
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Bacterial pathogens have evolved a sophisticated arsenal of virulence factors to modulate host cell biology. Enteropathogenic and enterohemorrhagic Escherichia coli (EPEC and EHEC) use a type III protein secretion system (T3SS) to inject microbial proteins into host cells. The T3SS effector cycle inhibiting factor (Cif) produced by EPEC and EHEC is able to block host eukaryotic cell-cycle progression. We present here a crystal structure of Cif, revealing it to be a divergent member of the superfamily of enzymes including cysteine proteases and acetyltransferases that share a common catalytic triad. Mutation of these conserved active site residues abolishes the ability of Of to block cell-cycle progression. Finally, we demonstrate that irreversible cysteine protease inhibitors do not abolish the Cif cytopathic effect, suggesting that another enzymatic activity may underlie the biological activity of this virulence factor. (C) 2008 Elsevier Ltd. All rights reserved.
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