RNA-based stable isotope probing provides no indication for rapid α-synuclein assimilation by murine gut bacteria.

Authors

Lena Brandau, Severin Weis, Maximilian Weyland, Fabian K Berger, Sylvia Schnell, Karl-Herbert Schäfer, Markus Egert

Published in

Access microbiology. Volume 4. Issue 5. Pages acmi000345. Epub May 04, 2022.

Abstract

In Parkinson's disease (PD), α-synuclein is a key protein in the process of neurodegeneration. Besides motor symptoms, most PD patients additionally suffer from gastrointestinal tract (GIT) dysfunctions, even several years before the onset of motor disabilities. Studies have reported a dysbiosis of gut bacteria in PD patients compared to healthy controls and have suggested that the enteric nervous system (ENS) can be involved in the development of the disease. As α-synuclein was found to be secreted by neurons of the ENS, we used RNA-based stable isotope probing (RNA-SIP) to identify gut bacteria that might be able to assimilate this protein. The gut contents of 24 mice were pooled and incubated with isotopically labelled (¹³C) and unlabelled (¹²C) α-synuclein. After incubation for 0, 4 and 24 h, RNA was extracted from the incubations and separated by density gradient centrifugation. However, RNA quantification of density-resolved fractions revealed no incorporation of the ¹³C isotope into the extracted RNA, suggesting that α-synuclein was not assimilated by the murine gut bacteria. Potential reasons and consequences for follow-up-studies are discussed.

PMID:
36003361
Bibliographic data and abstract were imported from PubMed on 15 Aug 2026.

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