The Molecular Cell recently published a research paper conducted by the University of Michigan which discovered a protein in E. coli that is capable of restricting the formation of toxic amyloids – a common element of debilitating diseases such as Parkinson’s. The formation of amyloids takes place when proteins form incorrectly, and they have the capacity to cause irreparable damage to brain tissue, even cellular death. The surprise findings by the University of Michigan researchers have the potential to lead to a therapeutic approach to the treatment of Parkinson’s and other neurodegenerative diseases, by targeting these amyloids.
Both Alzheimer’s and Parkinson’s share similarities in the way that amyloids affect them. However it has been found that E. coli and other cells are capable of assembling amyloids that are helpful to normal cellular function. The curli on the surface of E. coli cells have a protective role. These curli cause bacteria to stick to stomach walls in humans, thereby causing sickness. The beneficial amyloids that are produced by E. coli are not made inside the actual cell; therefore there is no toxicity for the bacteria.
There is something within E. coli that is capable of inhibiting the assemblage of amyloids within the cells. Since nothing takes place inside the cells, and protein synthesis takes place on the surface and is not toxic. Scientists conducted biochemical testing in order to understand precisely how E. coli blocked amyloids from forming within the cells. Ultimately a protein was discovered – CsgC – capable of inhibiting the formation of amyloids that are associated with diseases like Parkinson’s and Alzheimer’s.
The research also discovered another possibility. Curli could be targeted for invading biofilms – shields to deter antibiotics and antiseptics. Although E. coli bacteria have the capacity to cause chronic infections, the new discoveries could lead to drug therapy capable of retarding the biofilms and making the bacteria more vulnerable by treating them with molecules that block the formation of curli.