Abstract
Our study aims to investigate the physiological role of organophosphate hydrolase (OPH), hitherto known for its involvement in the degradation of organophosphate insecticides and nerve agents in Sphingobiumfuliginis. We find that OPH exists as part of the TonB-dependent Transport system that is involved in nutrient transport across the bacterial outer membrane. OPH interacts physically with the Ton complex components ExbD and TonB. The surface-exposed arginine residues (R91 and R96) of OPH facilitate its interaction with ExbD. OPH is targeted to the inner membrane of Escherichiacoli only when it is co-expressed with either ExbD or the ExbB/ExbD complex. In the absence of ExbD, OPH remains in the cytoplasm. Our findings suggest a role for OPH in outer membrane transport.
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