James Lauer

All Publications

• Effects of Phycosphere Bacteria on Their Algal Host Are Host Species-Specific and Not Phylogenetically Conserved MICROORGANISMS Baker, D., Lauer, J., Ortega, A., Jackrel, S. L., Denef, V. J. 2023; 11 (1)

  View details for DOI 10.3390/microorganisms11010062

  View details for Web of Science ID 000927716300001

• Mechanistic insights into the protective roles of polyphosphate against amyloid cytotoxicity. Life science alliance Lempart, J., Tse, E., Lauer, J. A., Ivanova, M. I., Sutter, A., Yoo, N., Huettemann, P., Southworth, D., Jakob, U. 2019; 2 (5)

  Abstract

  The universally abundant polyphosphate (polyP) accelerates fibril formation of disease-related amyloids and protects against amyloid cytotoxicity. To gain insights into the mechanism(s) by which polyP exerts these effects, we focused on α-synuclein, a well-studied amyloid protein, which constitutes the major component of Lewy bodies found in Parkinson's disease. Here, we demonstrate that polyP is unable to accelerate the rate-limiting step of α-synuclein fibril formation but effectively nucleates fibril assembly once α-synuclein oligomers are formed. Binding of polyP to α-synuclein either during fibril formation or upon fibril maturation substantially alters fibril morphology and effectively reduces the ability of α-synuclein fibrils to interact with cell membranes. The effect of polyP appears to be α-synuclein fibril specific and successfully prevents the uptake of fibrils into neuronal cells. These results suggest that altering the polyP levels in the extracellular space might be a potential therapeutic strategy to prevent the spreading of the disease.

  View details for DOI 10.26508/lsa.201900486

  View details for PubMedID 31533964

  View details for PubMedCentralID PMC6751573