Abstract

Protein aggregation and amyloid formation have historically been linked with various diseases such as Alzheimer’s and Parkinson’s disease, but recently functional amyloids have gained a great deal of interest in not causing a disease and having a distinct function in vivo. They provide different types of functionality ranging from virulence during infection to structural scaffolds in biofilm, to storage of peptide hormones, to formation of melanin granula in melanocytes, to memory storage and during cell death, and many others. Functional bacterial amyloids form the structural scaffold in bacterial biofilms occurrence of functional amyloids in the biofilm renders the biofilm impossible to disassemble, and hence it becomes impossible to treat the infection pharmacologically. The use of functional amyloids by bacteria provide a survival strategy for the bacteria along with antibiotic resistance.

Although functional amyloids are present in biofilms from different bacterial species the approach to forming functional amyloids is different for various bacteria. The Gram-positive methicillin-resistant Staphylococcus aureus, the most frequent cause of biofilm-associated infections, utilize several small amphipathic peptides, namely the phenol-soluble modulins (PSMs). This approach ensures relative biologically cheap building blocks for amyloid formation. The Gram-negative P. aeruginosa, involved in cystic fibrosis pathology forms functional amyloids composed primarily of a single protein, FapC. Functional amyloid formation by FapC assisted by auxiliary proteins arranged within the same operon. Using biophysical techniques we invertigate the formation of functional amyloids from both Gram-positive and Gram-negative bacteria to gain a better understanding of the molecular events taking place during amyloid formation.   

The talk is 45 minutes followed by 15 minutes of discussion, for a total of 1 hr.

Registration for a free sandwich no later than 1st May.

Biomedicine seminar organizing committee
Mikkel Vendelbo
Line Reinert
Søren Egedal Degn 
Martin Kristian Thomsen