AI Article Synopsis

  • Conidia possess a hydrophobic layer made of the hydrophobin protein RodA, which helps them resist drying out and reach lung tissue.
  • Researchers created various mutants to study the role of seven different hydrophobins, discovering that only RodA is essential for conidial hydrophobicity, structural integrity, and resistance to environmental stress.
  • The absence of rodlets (formed by RodA) on the conidial surface affects the fungus's drug sensitivity, highlighting RodA's crucial role in the cell wall properties of conidia.

Article Abstract

Resistance of conidia to desiccation and their capacity to reach the alveoli are partly due to the presence of a hydrophobic layer composed of a protein from the hydrophobin family, called RodA, which covers the conidial surface. In there are seven hydrophobins (RodA-RodG) belonging to class I and III. Most of them have never been studied. We constructed single and multiple hydrophobin-deletion mutants until the generation of a hydrophobin-free mutant. The phenotype, immunogenicity, and virulence of the mutants were studied. is the most expressed hydrophobin in sporulating cultures, whereas is upregulated in biofilm conditions and in vivo Only RodA, however, is responsible for rodlet formation, sporulation, conidial hydrophobicity, resistance to physical insult or anionic dyes, and immunological inertia of the conidia. None of the hydrophobin plays a role in biofilm formation or its hydrophobicity. RodA is the only needed hydrophobin in , conditioning the structure, permeability, hydrophobicity, and immune-inertia of the cell wall surface in conidia. Moreover, the defect of rodlets on the conidial cell wall surface impacts on the drug sensitivity of the fungus.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5872305PMC
http://dx.doi.org/10.3390/jof4010002DOI Listing

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