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Area of Science:

  • Biochemistry
  • Microbiology
  • Structural Biology

Background:

  • Nonenzymatic deamidation of asparagine (Asn) and glutamine (Gln) is a common post-translational modification impacting protein function.
  • Curli fibers, composed of CsgA protein, are crucial for bacterial biofilm formation.
  • CsgA's high Asn/Gln content makes it susceptible to deamidation, potentially affecting its self-aggregation properties.

Purpose of the Study:

  • To investigate the impact of nonenzymatic deamidation on the structure and function of CsgA.
  • To identify specific deamidation sites within CsgA.
  • To explore the potential of modulating CsgA deamidation for controlling biofilm formation.

Main Methods:

  • Mass spectrometry (LC-MS/MS) to monitor deamidation and identify modification sites.
  • Thioflavin T (ThT) fluorescence assays to measure amyloid fibril formation kinetics.
  • Circular dichroism (CD) spectroscopy to assess protein secondary structure.
  • Hydrogen-deuterium exchange (HDX) mass spectrometry to probe protein aggregation dynamics.

Main Results:

  • Identified extensive deamidation of Asn residues in CsgA, with "Asn-Gly" sites being particularly reactive.
  • Deamidated CsgA showed significantly reduced and slower amyloid fibril formation compared to wild-type CsgA, as evidenced by ThT assays and HDX-MS.
  • CD spectroscopy revealed that deamidated CsgA loses its ability to form amyloid structures and remains largely unstructured.

Conclusions:

  • Nonenzymatic deamidation of CsgA inhibits its fibrillization process and impairs its function in forming amyloid structures.
  • These findings highlight deamidation as a critical factor influencing curli biogenesis and biofilm architecture.
  • Targeting CsgA deamidation presents a potential therapeutic strategy to disrupt biofilm formation in relevant bacterial pathogens.