Amyloid Beta Requires Oligomerization to Limit the Growth of Salmonella enterica

Faculty Mentor(s)

Dr. Griffin, Biology

Document Type

Poster

Event Date

4-21-2017

Abstract

Alzheimer's Disease (AD) is the sixth leading cause of death in the United States. In fact, one out of every eight Americans age sixty-five and older will develop the disease. One pathological hallmark associated with AD and other forms of dementia is the over-accumulation of the amyloid beta peptide. This excess of amyloid beta leads to the peptide’s oligomerization, ultimately leading to neuronal loss. While amyloid beta is present at low levels in all humans, its function is a source of great debate. A growing number of reports has demonstrated that amyloid beta has antimicrobial properties. To extend these findings, we tested the hypothesis that amyloid beta exerts antimicrobial activity against Salmonella enterica (S. enterica). Additionally, our work tested whether 2-amino-4-chlorophenol (2a4cp), a compound that prevents amyloid beta oligomerization, affects the antimicrobial function of the peptide. After treating S. enterica with a range of concentrations (1pM-1μM) of both major isoforms of amyloid beta (1-40 and 1-42), we measured bacterial cell viability with the Alamar Blue assay. Our results revealed that the 1-42 isoform (F=32.91, p< 0.001), but not the 1-40 isoform of amyloid beta, limited bacterial growth. Moreover, 2a4cp co-administration decreased amyloid beta’s ability to limit the growth of S. enterica. Altogether, these findings indicate that amyloid beta oligomers are responsible for the antimicrobial abilities of amyloid beta.

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