Role of Bcl-2 Family Members in Caspase-Independent Apoptosis duringChlamydiaInfection

Open Access
Publisher Website
Google Scholar
Abstract
Infection with an obligate intracellular bacterium, theChlamydia trachomatislymphogranuloma venereum (LGV/L2) strain or the guinea pig inclusion conjunctivitis serovar ofChlamydia psittaci, leads to apoptosis of host cells. The apoptosis is not affected by a broad-spectrum caspase inhibitor, and caspase-3 is not activated in infected cells, suggesting that apoptosis mediated by these two strains ofChlamydiais independent of known caspases. Overexpression of the proapoptotic Bcl-2 family member, Bax, was previously shown to induce caspase-independent apoptosis, and we find that Bax is activated and translocates from the cytosol to the mitochondria inC. psittaci-infected cells.C. psittaci-induced apoptosis is inhibited in host cells overexpressing Bax inhibitor-1 and is inhibited through overexpression of Bcl-2, which blocks both caspase-dependent and -independent apoptosis. As Bax and mitochondria are ideally located to sense stress-related metabolic changes emanating from the interior of an infected cell, it is likely that Bax-dependent apoptosis may also be observed in cells infected with other intracellular pathogens.