Abstract:
:Inhibition of apoptotic response of host cells during an early phase of infection is a strategy used by many enteroinvasive bacterial pathogens to enhance their survival. Here, we report the identification of a soluble form of the pilus protein FimA from the culture supernatants of E. coli K1, Salmonella, and Shigella that can potently inhibit Bax-mediated release of cytochrome c from isolated mitochondria. Similar to the infected cells, HCT116 cells stably expressing FimA display a delay in the integration of Bax into outer mitochondrial membrane induced by apoptotic stimuli. FimA targets to mitochondria through binding to VDAC1, which is a prerequisite step for E. coli K1 to render the short-term blockade of apoptotic death in the host cells. Interestingly, FimA strengthens the VDAC1-hexokinase interaction and prevents dissociation of hexokinase from VDAC1 triggered by apoptotic stimuli. Together, these data thus reveal a paradigm of antiapoptosis mechanism undertaken by the enteroinvasive bacteria.
journal_name
Mol Celljournal_title
Molecular cellauthors
Sukumaran SK,Fu NY,Tin CB,Wan KF,Lee SS,Yu VCdoi
10.1016/j.molcel.2010.02.015subject
Has Abstractpub_date
2010-03-26 00:00:00pages
768-83issue
6eissn
1097-2765issn
1097-4164pii
S1097-2765(10)00165-6journal_volume
37pub_type
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