Selective protein aggregation confines and inhibits endotoxins in wounds: Linking host defense to amyloid formation
Clicks: 19
ID: 281397
2023
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
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| 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 |
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