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

ABSTRACT: 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 mode

SUBMITTER: Petrlova J 

PROVIDER: S-EPMC10561040 | biostudies-literature | 2023 Oct

REPOSITORIES: biostudies-literature