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Small GTPases of the Rab family are master regulators of membrane trafficking, responsible for coordinating the sorting, packaging and delivery of membrane-bound vesicles to specific sites within eukaryotic cells. The contribution of these proteins to the biology of the human pathogenic fungus  Aspergillus fumigatus  has not been explored. In this study, we characterized the  srgA  gene, encoding a Rab GTPase closely related to Sec4. We found that a GFP-SrgA fusion protein accumulated preferentially at hyphal tips and mature condiophores. The radial growth of a Δ srgA  mutant was impaired on both rich and minimal medium, consistent with a role for SrgA in filamentous growth. In addition, the Δ srgA  mutant revealed dysmorphic conidiophores that produced conidia with heterogeneous morphology. The Δ srgA  mutant was hypersensitive to brefeldin A-mediated inhibition of vesicular trafficking and showed increased temperature sensitivity relative to wild type  A. fumigatus . However, the most striking phenotype of this mutant was its phenotypic heterogeneity. Individual colonies isolated from the original Δ srgA  mutant showed variable morphology with colony sectoring. In addition, each isolate of the Δ srgA  mutant displayed divergent phenotypes with respect to thermotolerance,  in vitro  stress response and virulence in a  Galleria mellonella  infection model. Taken together, these results indicate that SrgA contributes to the asexual development and filamentous growth of  A. fumigatus . However, the discordant phenotypes observed among individual isolates of the Δ srgA  mutant suggest that the absence of  srgA  exerts selective pressure for the acquisition of compensatory changes, such as second-site suppressor mutations.

plos one

Deletion of the sec4 Homolog srgA from Aspergillus fumigatus Is Associated with an Impaired Stress Response, Attenuated Virulence and Phenotypic Heterogeneity