Exacerbated salmonellosis in poly(ADP-ribose) polymerase 14-deficient mice

Eukaryotic cells rely on dynamic cell-signaling mechanisms to mount responses to external perturbations, such as an invading bacterial pathogen. The PARP protein family is a group of enzymes catalyzing a protein post-translational modification known as ADP-ribosylation. PARP1, the founding member, has received considerable research interest, in particular in cancer. However, recent data imply that PARP1 and, in particular, the other PARPs have regulatory functions in inflammatory responses. Yet, the mechanistic basis and, more importantly, the physiological relevance have largely remained elusive. Our study with the systemic Parp14-deficient mice provides compelling <i>in vivo</i> evidence that Parp14 is an integral part of the physiological response to <i>S.</i> Typhimurium infection.