Phytophthora cinnamomi is a pathogenic oomycete that poses a significant threat to global biodiversity. It causes tree death and loss of vegetation/ crops by attaching to the fine-feeder roots and releasing apoplastic and cytosolic effectors. The destructive nature of these effectors during plant-pathogen interactions drives a complex array of defense responses and when successful, the pathogen causes plant death. Phytophthora cinnamomi exhibits various life stages, which enable it to survive through harsh environments. This has contributed to its success as a pathogen as it takes advantage of weakened potential hosts.
However, the molecular mechanism of P. cinnamomi pathogenicity is not well-understood. In order to better understand the pathogen, a proteomic approach was used to dissect sub-cellular proteomes of P. cinnamomi. We were able to extract high quality intracellular and secreted proteins of P. cinnamomi and perform preliminary analysis of the intracellular proteome using gel-free shotgun proteomics. We identified 612 unique proteins when the mass spectrum was matched against the P. cinnamomi genome. From here, a 2-dimensional separation by reverse phase chromatography and liquid chromatography mass spectrometry will be developed to analyse the intracellular and secreted proteomes. We anticipate this approach will lead to a greater level of protein identification and provide a comprehensive biochemical snapshot of the pathogen.