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Abstract:
Diverse members of the bacterial order Chlamydiales cause severe diseases in humans. Chlamydiales cannot survive and reproduce outside of host cells, due to the complete loss of several biosynthetic pathways, but rely on specialized transport systems to import the corresponding metabolites from the host. We performed a detailed biochemical analysis of a purified recombinant ATP/ADP transporter from the Chlamydia-related bacterium Protochlamydia amoebophila (PamNTT1). Our studies revealed that PamNTT1 favours ATP import into vesicles loaded with ADP, whereas the exchange of ATP in the opposite direction is negligible. Furthermore, we demonstrated that PamNTT1, in contrast to the mitochondrial ADP/ATP carrier, is independent of a membrane potential. The identified biochemical characteristics of PamNTT1 appear to be a sophisticated adaptation to the requirements of the intracellular lifestyle of P. amoebophila, serving to facilitate effective energy parasitism.
