Structural insights into functional amyloid inhibition in Gram -ve bacteria

Biochem Soc Trans. 2016 Dec 15;44(6):1643-1649. doi: 10.1042/BST20160245.

Abstract

Amyloids are proteinaceous aggregates known for their role in debilitating degenerative diseases involving protein dysfunction. Many forms of functional amyloid are also produced in nature and often these systems require careful control of their assembly to avoid the potentially toxic effects. The best-characterised functional amyloid system is the bacterial curli system. Three natural inhibitors of bacterial curli amyloid have been identified and recently characterised structurally. Here, we compare common structural features of CsgC, CsgE and CsgH and discuss the potential implications for general inhibition of amyloid.

Keywords: Fap; amyloid inhibitors; curli; functional amyloid.

Publication types

  • Review

MeSH terms

  • Amyloid / chemistry
  • Amyloid / metabolism*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism*
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / metabolism*
  • Membrane Transport Proteins / chemistry
  • Membrane Transport Proteins / metabolism
  • Models, Molecular
  • Protein Conformation
  • Static Electricity

Substances

  • Amyloid
  • Bacterial Proteins
  • CsgC protein, E coli
  • CsgE protein, E coli
  • Escherichia coli Proteins
  • Membrane Transport Proteins
  • Crl protein, Bacteria