strains isolated from healthy individuals did not cause the same level of protein accumulation. While the clumps formed by these bacteria strains in Parkinson's disease patients were also found to be larger.
“Our findings make it possible to screen for the carriers of these harmful Desulfovibrio bacteria. Consequently, they can be targeted by measures to remove these strains from the gut, potentially alleviating and slowing the symptoms of patients with Parkinson’s disease. Once the Desulfovibrio bacteria are eliminated from the gut, α-synuclein aggregates are no longer formed in intestinal cells, from which they travel towards the brain via the vagus nerve like prion proteins,” concludes Saris.
The study is conducted by researchers from the University of Helsinki and the University of Eastern Finland. The study has been published in the journalIntroduction: The aggregation of the neuronal protein alpha-synuclein is a key feature in the pathology of Parkinson’s disease . Alpha-syn aggregation has been suggested to be induced in the gut cells by pathogenic gut microbes such as Desulfovibrio bacteria, which has been shown to be associated with PD.
Methods: Fecal samples of ten PD patients and their healthy spouses were collected for molecular detection of Desulfovibrio species, followed by bacterial isolation. Isolated Desulfovibrio strains were used as diets to feed Caenorhabditis elegans nematodes which overexpress human alpha-syn fused with yellow fluorescence protein. Curli-producing Escherichia coli MC4100, which has been shown to facilitate alpha-syn aggregation in animal models, was used as a control bacterial strain, and E.
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