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SUMMARY:Functional Protein Fibrils in the Fight Against Pathogens - Prof. 
 Meytal Landau\, Technion-Israel Institute of Technology
DTSTART:20210602T093000Z
DTEND:20210602T103000Z
UID:TALK159967@talks.cam.ac.uk
CONTACT:Anne Jacobs
DESCRIPTION:Different organisms secrete proteins and peptides that self-as
 semble into ordered amyloid fibrils that carry various physiological roles
 . Their function as key virulence factors in microbes\, has rendered them 
 attractive candidates for structural characterization aimed at discovering
  novel antimicrobial therapeutics.  In contrast to the vast structural inf
 ormation available on eukaryotic amyloids involved in neurodegenerative an
 d systemic diseases or which serve specific physiological roles\, high-res
 olution structural information on microbial amyloids is lacking\, perhaps 
 due to their polymorphic nature and relatively recent discovery. Our lab p
 ioneered the atomic-level analysis of bacterial amyloids and other eukaryo
 tic functional fibrils involved in cytotoxicity\, biofilm structuring\, an
 d antibacterial activity\, and uncovered novel morphologies\, extending be
 yond the canonical amyloid cross- structural feature composed of tightl
 y mated β-sheets (Tayeb-Fligelman et. al.\, Science 2017\, Salinas et al.
 \, Nat Commun 2018\, Perov et al.\, PLoS Pathogens 2019\, Tayeb-Fligelman 
 et al.\, Structure 2020\, Salinas et. al.\, PNAS 2021\, Engelberg and Land
 au\, Nat Commun 2020\, and unpublished results).  The findings include cro
 ss-α fibrils of stacked α-helices arranged in mated sheets\, just as in 
 cross-β fibrils\, cross-a/β secondary structure polymorphism in the same
  sequence\, and other densely packed helical fibrils with novel morphologi
 es. The similar structures of biofilm-associated and human pathological am
 yloidogenic regions led to repurposing of anti-Alzheimer’s compounds to 
 act against Salmonella biofilm. Moreover\, the structural similarity impli
 es on possible inter-species interactions that could have bearing on amylo
 id diseases by the creation of transmissible agents. We expect that a deta
 iled molecular understanding of microbial amyloids and other functional fi
 brils will provide the foundation for understanding the etiology of and po
 tential connection between microbial and human ‘amylomes’ in health an
 d disease. 
LOCATION:https://zoom.us/j/96842517234
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