pH- and concentration-dependent supramolecular assembly of a fungal defensin plectasin variant into helical non-amyloid fibrils

Christin Pohl (), Gregory Effantin, Eaazhisai Kandiah, Sebastian Meier, Guanghong Zeng, Werner Streicher, Dorotea Raventos Segura, Per H. Mygind, Dorthe Sandvang, Line Anker Nielsen, Günther H. J. Peters, Guy Schoehn, Christoph Mueller-Dieckmann, Allan Noergaard and Pernille Harris ()
Additional contact information
Christin Pohl: Novozymes A/S
Gregory Effantin: Univ. Grenoble Alpes, CNRS, CEA, Institute for Structural Biology
Eaazhisai Kandiah: European Synchrotron Radiation Facility
Sebastian Meier: Technical University of Denmark, Department of Chemistry
Guanghong Zeng: DFM A/S (Danish National Metrology Institute)
Werner Streicher: Novozymes A/S
Dorotea Raventos Segura: Novozymes A/S
Per H. Mygind: Novozymes A/S
Dorthe Sandvang: Novozymes A/S
Line Anker Nielsen: Novozymes A/S
Günther H. J. Peters: Technical University of Denmark, Department of Chemistry
Guy Schoehn: Univ. Grenoble Alpes, CNRS, CEA, Institute for Structural Biology
Christoph Mueller-Dieckmann: European Synchrotron Radiation Facility
Allan Noergaard: Novozymes A/S
Pernille Harris: Technical University of Denmark, Department of Chemistry

Nature Communications, 2022, vol. 13, issue 1, 1-15

Abstract: Abstract Self-assembly and fibril formation play important roles in protein behaviour. Amyloid fibril formation is well-studied due to its role in neurodegenerative diseases and characterized by refolding of the protein into predominantly β-sheet form. However, much less is known about the assembly of proteins into other types of supramolecular structures. Using cryo-electron microscopy at a resolution of 1.97 Å, we show that a triple-mutant of the anti-microbial peptide plectasin, PPI42, assembles into helical non-amyloid fibrils. The in vitro anti-microbial activity was determined and shown to be enhanced compared to the wildtype. Plectasin contains a cysteine-stabilised α-helix-β-sheet structure, which remains intact upon fibril formation. Two protofilaments form a right-handed protein fibril. The fibril formation is reversible and follows sigmoidal kinetics with a pH- and concentration dependent equilibrium between soluble monomer and protein fibril. This high-resolution structure reveals that α/β proteins can natively assemble into fibrils.

Date: 2022
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DOI: 10.1038/s41467-022-30462-w

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