Selective protein aggregation confines and inhibits endotoxins in wounds: Linking host defense to amyloid formation

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ID: 281397
2023
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Abstract
Summary: Bacterial lipopolysaccharide (LPS) induces rapid protein aggregation in human wound fluid. We aimed to characterize these LPS-induced aggregates and their functional implications using a combination of mass spectrometry analyses, biochemical assays, biological imaging, cell experiments, and animal models. The wound-fluid aggregates encompass diverse protein classes, including sequences from coagulation factors, annexins, histones, antimicrobial proteins/peptides, and apolipoproteins. We identified proteins and peptides with a high aggregation propensity and verified selected components through Western blot analysis. Thioflavin T and Amytracker staining revealed amyloid-like aggregates formed after exposure to LPS in vitro in human wound fluid and in vivo in porcine wound models. Using NF-κB-reporter mice and IVIS bioimaging, we demonstrate that such wound-fluid LPS aggregates induce a significant reduction in local inflammation compared with LPS in plasma. The results show that protein/peptide aggregation is a mechanism for confining LPS and reducing inflammation, further emphasizing the connection between host defense and amyloidogenesis.
Reference Key
petrlova2023selectiveiscience Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Petrlova, Jitka;Hartman, Erik;Petruk, Ganna;Lim, Jeremy Chun Hwee;Adav, Sunil Shankar;Kjellström, Sven;Puthia, Manoj;Schmidtchen, Artur;
Journal iScience
Year 2023
DOI
DOI not found
URL
http://www.sciencedirect.com/science/article/pii/S258900422302028X
Keywords
Medicine Science Dentistry Immunologic diseases. Allergy environmental sciences toxicology. poisons agriculture genetics cytology animal culture diseases of the digestive system. gastroenterology

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