Figure 1

PD0956 functional characterization.
(a) Schematic representation of the coding region of PD0956 including the 28 amino acid N-terminal signal peptide (MRAIKLNKLSLGLLGIFSLTLIPSLSIA) and the position of the predicted catalytic active residues (H146, D194, S280). (b) Superimposition of predicted structures for PD0956 (protein in green, catalytic residues in red) and an extracellular alkaline serine protease (PDB: 3CP7A, protein in purple, residues in yellow) showing the conserved catalytic triad. The serine residue overlaps completely (in black). Superimposition was carried out using MUSTANG. (c) Immunogold labeling of X. fastidiosa PD0956. Gold particles are associated with the bacterial secreted matrix (black arrowheads). (d) Protease activity for wild type PD0956 expressed in E. coli (pJX-prtA), an empty vector control and the PD0956 functional mutant (pJX-prtA-S280A). The functional mutant contains a substitution in the predicted catalytic residue. Activity was quantified using fluorescein labeled casein as substrate. Average values and standard deviations of three independent experiments are plotted (*p-value < 0.05, two-tailed T-test).