A zinc metalloprotease inhibitor, Inh, from the insect pathogen Photorhabdus luminescens.

Abstract

The entomopathogen Photorhabdus luminescens secretes many proteins during the late stages of insect larvae infection and during in vitro laboratory culture. The authors have previously characterized and purified a 55 kDa zinc metalloprotease, PrtA, from culture supernatants of P. luminescens. PrtA is secreted via a classical type I secretory pathway and is encoded within the operon prtA-inh-prtBCD. The 405 bp inh gene encodes a 14.8 kDa pre-protein that is translocated to the periplasm by the classical signal-peptide-dependent sec pathway, yielding the mature 11.9 kDa inhibitor Inh. Inh is a specific inhibitor of the protease PrtA. This study describes the purification of Inh and the initial characterization of its in vitro protease inhibition properties.