Browsing by Subject "Aβ1-42"

Alzheimer’s disease (AD) is the seventh leading cause of death worldwide. One hallmark of AD includes the amyloid beta (Aβ1-42) peptide that accumulates into oligomers, fibrils, and plaques. Aβ1-42 has been shown to be structurally and functionally similar to antimicrobial peptides (AMPs). Publications have reported that Borrelia burgdorferi can be found in the brain of AD patients. B. burgdorferi and B. garinii cause Lyme disease (LD). B. duttonii is responsible for relapsing fever (RF), a disease characterized by recurrent episodes of high fever. The aim of this research was to study whether synthetic Aβ1-42 binds to LD and RF Borrelia sp. and several bacterial molecules important for their virulence, and whether Borrelia sp. have evolved strategies to evade Aβ1-42-mediated killing. Binding of Aβ1-42 to B. burgdorferi, B. garinii and B. duttonii and several microbial molecules was studied by ELISA and immunoblotting. Bacterial culturing and microscopy were used to study survival, agglutination, and phagocytosis of Borrelia sp. in the presence of Aβ1-42 and microglia. In this research, Aβ1-42 was able to bind and agglutinate all of the three studied Borrelia sp. However, Aβ1-42 reduced the survival and increased the phagocytosis of B. duttonii. while B. burgdorferi and B. garinii were unaffected. In addition, potential Aβ1-42 binding molecules were detected from several bacterial species, including FhbA expressed by B. duttonii. In conclusion, this study suggests that some restricted species of bacteria may evade Aβ1-42 entrapment and thus may be involved in the ability of the species to invade the CNS that may trigger neuroinflammation related to AD.