中国神经再生研究(英文版) ›› 2023, Vol. 18 ›› Issue (5): 1027-1028.doi: 10.4103/1673-5374.355757

• 观点:退行性病与再生 • 上一篇    下一篇

LL-37和CsgC例证了抗淀粉样蛋白、抗微生物和抗生物膜蛋白活性之间的串扰

  

  • 出版日期:2023-05-15 发布日期:2022-11-01

LL-37 and CsgC exemplify the crosstalk between anti-amyloid, antimicrobial, and anti-biofilm protein activities

Jaime Santos, Salvador Ventura*, Irantzu Pallarès*   

  1. Institut de Biotecnologia i Biomedicina, Departament de Bioquímica i Biologia Molecular, Universitat Autònoma de Barcelona, Bellaterra, Barcelona, Spain
  • Online:2023-05-15 Published:2022-11-01
  • Contact: Salvador Ventura, PhD, salvador.ventura@uab.es; Irantzu Pallarès, PhD, irantzu.pallares@uab.cat.

Abstract: Protein misfolding and aggregation into amyloid fibrils is the main pathological hallmark of neurodegenerative diseases, including Alzheimer’s, Parkinson’s, Huntington’s, and prion diseases (Chiti and Dobson, 2017). These insoluble fibrillar deposits possess a common structure characterized by a cross-β-sheet conformation in which β-strands run transversely to the fiber axis and form an intermolecular network of hydrogen bonds. However, amyloid formation is not only found in disease; the unique properties of this protein fold are also exploited by nature to perform a growing list of relevant and highly conserved cellular functions (Otzen and Riek, 2019). Pathogenic and functional amyloid formation needs to be regulated to sustain organism fitness, and a wide range of strategies have evolved to prevent uncontrolled aggregation. Importantly, we are not only exposed to our endogen amyloidogenic proteins, but we also face the threat of food and bacterial amyloids. For instance, many bacterial species in the gut microbiome can form an amyloid scaffolded biofilm, which facilitates bacterial proliferation, promotes the synergy between the host and the microbiome, and may eventually play a role in the pathogenesis of different diseases. It is then plausible to speculate that our own systemic defense against endogenous amyloids can work to fight this exogenic risk. Indeed, given the common structural properties shared by unrelated amyloids, it could be expected that the same cellular agents would mediate the response to human amyloids and those from other sources. In this perspective, we provide context for this idea by exploring the overlap between anti-microbial, anti-biofilm, and anti-amyloid activities, defining a framework for developing novel therapies for neurodegenerative diseases.