Mitochondrial membrane permeabilization (MMP) is a critical step of several
apoptotic pathways. Some infectious intracellular pathogens can regulate (
induce or inhibit) apoptosis of their host cells at the mitochondrial level
, by targeting proteins to mitochondrial membranes that either induce or in
hibit MMP. Pathogen-encoded mitochondrion-targeted proteins may or may not
show amino acid sequence homology to Bcl-2-like proteins. Among the Bcl-2-u
nrelated, mitochondrion-targeted proteins, several interact with the voltag
e-dependent anion channel (VDAC) or with the adenine nucleotide translocato
r (ANT). While VDAC-targeted proteins show homology to VDAC/porin, ANT-targ
eted proteins possess relatively short cationic binding domains, which may
facilitate insertion into the negatively charged inner mitochondrial membra
ne. It may be speculated that such proteins employ pre-existing host-intrin
sic mechanisms of MMP control.