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New clues into the self-assembly of Vmh2, a basidiomycota class I hydrophobin

Anna Pennacchio1, Paola Cicatiello1, Eugenio Notomista2

  • 1Department of Chemical Sciences, University of Naples "Federico II", via Cintia 4, I-80126 Naples, Italy.

Biological Chemistry
|June 14, 2018
PubMed

Insights

Class I hydrophobins self-assemble into amyloid-like fibrils. This study investigated Vmh2 mutants, revealing a specific loop destabilization triggers fibril formation via a beta-hairpin intermediate.

Area of Science:

  • Biochemistry
  • Mycology
  • Structural Biology

Background:

  • Hydrophobins are fungal proteins forming amphiphilic films at interfaces.
  • Class I hydrophobin aggregates share structural similarities with amyloid fibrils.

Purpose of the Study:

  • To identify molecular determinants of Class I hydrophobin self-assembly.
  • To characterize site-directed mutants of the Class I hydrophobin Vmh2.

Main Methods:

  • Site-directed mutagenesis of Vmh2.
  • Characterization of Vmh2 mutants to study self-assembly.

Main Results:

  • Five Vmh2 mutants were designed and characterized.
  • A mechanism for Vmh2 fibril formation was proposed, involving loop destabilization and beta-hairpin formation.

Conclusions:

  • Specific loop destabilization is a key event in Class I hydrophobin fibril formation.
  • The formation of a beta-hairpin initiates the beta-spine of amyloid fibrils.
Keywords:
3D modelamyloid fibrilsfibril formationsite-directed mutantssurface adhesion

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