1887

Abstract

Previously, 12 protease-deficient mutants of the pv. () RS105 strain were recovered from a Tn-tagged mutant library. In the current study, the Tn insertion site in each mutant was mapped. Mutations in genes encoding components of the type II secretion apparatus, cAMP regulatory protein, integral membrane protease subunit, -adenosylmethionine decarboxylase proenzyme and extracellular protease () either partially or completely abolished extracellular protease activity (ECPA) and reduced virulence in rice. Transcription of was induced in all the mutants except RΔ Complementation of RΔ with restored ECPA, virulence and bacterial growth . Purified EcpA induced chlorosis- and necrosis-like symptoms similar to those induced by the pathogen when injected into rice leaves. Heterologous expression of conferred ECPA upon the vascular bacterium pv. () and upon non-pathogenic . Genetic analysis demonstrated that the C-terminal residues of EcpA in PXO99 and RS105 are different, and a frame shift in may explain the absence of EcpA activity in . Collectively, these results suggest that EcpA is a tissue-specific virulence factor for but not , although the two pathovars are closely related bacterial pathogens of rice.

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2012-09-01
2024-04-19
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