Fig. 3

Bioinformatic and phenotypic analyses of HrpP from E. amylovora. a Schematic representation of T3S4 domain protein alignment from animal and plant pathogenic bacteria. The length of the lines and boxes represent the actual sizes of the protein and domain. Numbers indicate amino acid position. HrpP in E. amylovora is markedly smaller than T3S4 proteins in animal bacterial pathogens and the flagellum. b Visualization of T3S4 protein sequence alignments with Weblogo software demonstrates that HrpP exhibits a conserved P-X-L-G motif characteristic of T3S4 proteins. c WT Ea1189 and Ea1189∆hrpP inoculated into immature pear fruits and N. benthamiana. Pear fruit necrosis was recorded 6 days post inoculation while the hypersensistive response in N. benthamiana was observed 16 h post inoculation. HrpP is a pathogenicity factor required for HR elicitation