, 2009). The presence of sphingolipid based signal transduction pathway in A. nidulans, and its role in fungal development has previously been observed (Li et al., 2007). In a localization study, AfuNCE102-EGFP fusion protein showed a reticulotubular distribution representing ER localization. This is similar to the cellular localization of NCE102 in yeast reported by Kumar et al. (2002) and the cytoplasmic distribution of another eisosomal transmembrane protein, SurG, in A. nidulan (Vangelatos et al., 2010). The localization of AfuNce102 to ER was more prominent in the basal region of elongated hyphae with frequent ring-like

structures that represent the ER envelope around the nuclei. This may indicate Selisistat cost the accumulation of AfuNce102 protein in older regions of hyphae over time. EGFP fluorescent was also observed along the septa. This could be due to the strategic positioning of ER as a supplying center of material for septum formation as suggested by Maruyama et al. (2006). Alternatively, AfuNce02-EGFP may be directly targeted to the septum or trapped in the septum

during septum formation. During conidiogenesis, AfuNce102 localized to conidiophores and mature conidia. This is consistent with the results presented by Vangelatos et al. (2010), which demonstrate the co-localization of eisosomal proteins during conidiogenesis. In A. nidulans, the eisosomal proteins, PilA, PilB, and SurG, are localized at the periphery of resting conidia, and it selleck chemicals Phosphoglycerate kinase is expected that the transmembrane protein, AfuNce102, co-localizes with eisosomes as reported

previously. The virulence of AfuNce102 deletion mutant was comparable to that of the wild type. This suggests that AfuNce102 is not required for pathogenesis in the systemic infection model used in the present study. In conclusion, we have shown that AfuNce102 is involved in sporulation process in A. fumigatus. Although the localization data presented in this study were derived from the expression of AfuNce102-GFP under the control of a strong and nonphysiological promoter, the targeting of GFP fusion protein to the conidiophores and mature conidia along with an abnormal sporulation in deletion mutant may be relevant to the potential role in sporulation. This work was supported by grant No. 486 from Pasteur Institute of Iran. ”
“Syringomycin E is a cyclic lipodepsipeptide produced by strains of the plant bacterium Pseudomonas syringae pv. syringae. Genetic studies involving the yeast Saccharomyces cerevisiae have revealed that complex sphingolipids play important roles in the action of syringomycin E.