Premium
Oligopeptide permease is required for expression of the Bacillus thuringiensis plcR regulon and for virulence
Author(s) -
Gominet Myriam,
Slamti Leyla,
Gilois Nathalie,
Rose Matthias,
Lereclus Didier
Publication year - 2001
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.2001.02440.x
Subject(s) - biology , regulon , permease , virulence , mutant , operon , tn10 , genetics , bacillus thuringiensis , gene , transposable element , microbiology and biotechnology , bacteria
PlcR is a pleiotropic regulator of virulence factors in the insect pathogen Bacillus thuringiensis and in the opportunistic human pathogen Bacillus cereus . It activates the transcription of at least 15 genes encoding extracellular proteins, including phospholipases C, proteases and enterotoxins. Expression of the plcR gene is autoregulated and activated at the onset of stationary phase. Here, we used mini‐Tn 10 transposition to generate a library of B. thuringiensis mutants, with the goal of characterizing genes involved in the expression of the plcR gene. Three mutant strains were identified carrying distinct mini‐Tn 10 insertions. The mutations impaired plcR expression and caused a deficient haemolytic phenotype, similar to the phenotype of a B. thuringiensis strain in which the plcR gene had been disrupted. The insertion sites of the three mini‐Tn 10 transposons mapped in a five‐gene operon encoding polypeptides homologous to the components of the oligopeptide permease (Opp) system of Bacillus subtilis , and with a similar structural organization. By analogy, the five B. thuringiensis genes were designated oppA , B , C , D and F . In vitro disruption of the B. thuringiensis oppB gene reproduced the effect of the mini‐Tn 10 insertions (i.e. the loss of haemolytic activity) and reduced the virulence of the strain against insects. These phenotypes are similar to those of a Δ plcR mutant. Opp is required for the import of small peptides into the cell. Therefore, plcR expression might be activated at the onset of stationary phase by the uptake of a signalling peptide acting as a quorum‐sensing effector. The opp mutations impaired the sporulation efficiency of B. thuringiensis when the cells were cultured in LB medium. Thus, Opp is on the pathway that ultimately regulates Spo0A phosphorylation, as is the case in B. subtilis. However, analysis of plcR expression in Δ oppB , Δ spo0A and Δ oppB Δ spo0A mutants indicates that Opp is required for plcR expression via a Spo0A‐independent mechanism.