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.
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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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