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Sequence-Encoded Aggregation of AA10 LPMO Domains as a Basis for Inclusion Body Design.

Ahmad Muaaz Hassan Butt1, Anwar Sunna1,2

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Summary

The N-terminal auxiliary activity family 10 (AA10) lytic polysaccharide monooxygenase (LPMO) domain from C. cellulovorans consistently forms inclusion bodies (IBs). This study shows that this aggregation tendency is conserved across homologous AA10 LPMO domains, supporting their use as scaffolds for protein nanoparticles.

Keywords:
AA10 homologuesaggregation-prone motifsbiofunctional nanomaterialshistidine braceinclusion bodiesprotein self-assembly

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Area of Science:

  • Biochemistry
  • Biotechnology
  • Materials Science

Background:

  • Inclusion bodies (IBs) in *Escherichia coli* are recognized as nanostructured materials with tunable properties.
  • The N-terminal auxiliary activity family 10 (AA10) lytic polysaccharide monooxygenase (LPMO) domain from *Caldibacillus cellulovorans* (Ccelp40) forms IBs and can generate functional IBs when fused to other proteins.

Purpose of the Study:

  • To investigate if the strong aggregation propensity of Ccelp40 is a general characteristic of AA10 LPMO domains.
  • To explore the potential of AA10 domains as scaffolds for protein-based nanomaterials.

Main Methods:

  • Heterologous expression of four homologous AA10 LPMO domains from distinct microorganisms in *E. coli* under identical cytosolic conditions.
  • Analysis of protein accumulation in insoluble fractions using SDS-PAGE densitometry.
  • Characterization of inclusion body morphology and structure using field-emission scanning electron microscopy and Fourier-transform infrared spectroscopy.

Main Results:

  • All tested AA10 LPMO homologues predominantly accumulated in the insoluble fraction, forming uniform inclusion bodies (IBs) with sub-micron diameters (550-860 nm).
  • IBs exhibited moderate polydispersity (0.45-0.54) and were characterized as compact spherical aggregates with β-sheet-enriched secondary structures.
  • The pronounced aggregation tendency of Ccelp40 was found to be conserved across the examined AA10 homologues.

Conclusions:

  • The AA10 LPMO domain exhibits a conserved, strong aggregation propensity across diverse microorganisms.
  • This conserved characteristic positions the AA10 domain as a promising scaffold for developing stable and recyclable protein nanoparticles.
  • The findings provide a comparative foundation for future biotechnological applications utilizing inclusion bodies.