Localisation of phosphoinositides in the grass endophyte Epichloe festucae and genetic and functional analysis of key components of their biosynthetic pathway in E. festucae symbiosis and Fusarium oxysporum pathogenesis

• Type: Article in International Scientific Journal
• Date: 2022

Authors

Hassing, B (Author) Other; Candy, A (Author) Other; Eaton, CJ (Author) Other; Fernandes, TR (Author) FCUP; Mesarich, CH (Author) Other; Di Pietro, A (Author) Other; Scott, B (Author) Other

Journal

Title: Fungal Genetics and Biology

Vol. 159

ISSN: 1087-1845

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 2 Citations

Other information

Authenticus ID: P-00W-H09

DOI: 10.1016/j.fgb.2022.103669

Abstract (EN): Phosphoinositides (PI) are essential components of eukaryotic membranes and function in a large number of signaling processes. While lipid second messengers are well studied in mammals and yeast, their role in filamentous fungi is poorly understood. We used fluorescent PI-binding molecular probes to localize the phosphorylated phosphatidylinositol species PI[3]P, PI[3,5]P2, PI[4]P and PI[4,5]P2 in hyphae of the endophyte Epichloe center dot festucae in axenic culture and during interaction with its grass host Lolium perenne. We also analysed the roles of the phosphatidylinositol-4-phosphate 5-kinase MssD and the predicted phosphatidylinositol-3,4,5triphosphate 3-phosphatase TepA, a homolog of the mammalian tumour suppressor protein PTEN. Deletion of tepA in E. festucae and in the root-infecting tomato pathogen Fusarium oxysporum had no impact on growth in culture or the host interaction phenotype. However, this mutation did enable the detection of PI[3,4,5]P3 in septa and mycelium of E. festucae and showed that TepA is required for chemotropism in F. oxysporum. The identification of PI[3,4,5]P3 in Delta tepA strains suggests that filamentous fungi are able to generate PI[3,4,5]P3 and that fungal PTEN homologs are functional lipid phosphatases. The F. oxysporum chemotropism defect suggests a conserved role of PTEN homologs in chemotaxis across protists, fungi and mammals.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 15