Proteomic analysis of phytopathogenic fungus Macrophomina phaseolina identify known and novel mycelial proteins with roles in growth and virulence

Abstract

Macrophomina phaseolina is a haploid, monotypic and clonally reproducing necrotrophic phytopathogenic fungus with widespread geographic distribution. Mycelia of this ascomycete play important role in propagation and pathogenicity providing insights into the mechanism of fungal growth and development. Despite its importance, proteomic analysis of Macrophomina mycelia is still not studied. Here, we have developed the first reference mycelial proteome map of M. phaseolina using 1-DE followed by MS/MS analysis. In total, 853 mycelial proteins were identified in three biological replicates. Gene ontology annotation depicted that most of these proteins function in biological processes related to translation and transcription initiation. In terms of molecular function, oxidoreductase activity represents the major biochemical reactions in fungal mycelia. KEGG pathway analysis further revealed that the mycelial proteins were primarily involved in metabolism, genetic information- and environmental information processing. Interestingly, 392 mycelial proteins were found to be involved in growth and virulence followed by 268 proteins in nutrient synthesis and translocation. Further, we examined the proteome data using network analysis that identified significant functional protein hubs centered on novel PCI domain-containing protein and known aconitate hydratase, oxidoreductase and pyruvate decarboxylase. This study reports the Macrophomina mycelial protein network that provides useful resource to further characterize mycelial proteins towards enhanced understanding of phytopathogenic fungal biology.