Comparative proteome profile of ungerminated spores and mycelium of the fungus Moniliophthora roreri, causal agent of frosty pod rot disease in cacao

Abstract

AbstractMoniliasis caused by the fungus Moniliophthora roreri is one of the most destructive cacao diseases in tropical America. In 2021, the presence of the pathogen was confirmed in cacao plantations in Brazil. This is the first proteomic study of the M. roreri protein profile of ungerminated spores and mycelium compared by 2D SDS‐PAGE (Two‐dimensional gel electrophoresis) associated with mass spectrometry. A total of 446 spots were detected on ungerminated spores gels and 402 spots on M. roreri mycelial gels. A total of 29 proteins were identified from the ungerminated spores, 21 of them were exclusive, and 53 were identified in the mycelium, 16 of them were exclusive. Most of the identified proteins at both development stages were categorized as being involved in metabolic processes, reduction/oxidation processes, and protein synthesis and folding. The interaction networks observed expand the known interactions of these proteins, resulting in eight functional clusters for proteins identified in ungerminated spores and seven clusters for mycelial proteins. In addition, a biological model of ungerminated spores and mycelium with cell location of proteins was constructed. The results contribute to a better understanding of the metabolic mechanisms of M. roreri during dormancy and vegetative development, which can support future studies for strategies to control moniliasis.