Poster #RP217
Molecular models for four class I hydrophobins from Crinipellis perniciosa: the causal agent of witches broom disease.
Monzani Paulo*, Stênio Santos*, Ramon Vidal*, Júlio Cascardo*
*UESC/DCB, Ilhéus, Brzail
Crinipellis perniciosa is the causal agent of witches broom disease of Threobroma cacao. Four Class I hydrophobins were identified for C. perniciosa genome and sequenced. Hydrophobins are a large family of secreted proteins with low molecular mass (7 -9 kDa), unique to filamentous fungi. These proteins have biophysical properties and function by self-assembling into amphipathic polymeric films at the interface between hydrophobic and hydrophilic surface. C. perniciosa hydrophobins codifies four proteins, with ranges of 22% to 28% of identities with the sequence Neurospora crassa hydrophobin. C. perniciosa have around 8 to 12 amino acids more than N. crassa. The molecular models for hydrophobins was built using the MODELLER program based in the structure of N. crassa class I hydrophobin. The models were validated using both Procheck and Verify 3D programs. The models were superposed with N. crassa hydrophobin to analyze the structures differences. The overall folds were partially maintained and the main differences were observed in the flexible loops and in the regions of amino acids insertion observed in the alignment, with high rmsd between structures. The model cph1 was used to docking with HEX program and in some solutions display amphipathic surfaces, consistent with the properties of the rodlets.