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Inhibition of Streptococcus mutans amyloid fibril formation by cranberry fractions
Author(s) -
Adamec Asher B,
Helm Kyle P,
Crowley Paula J,
Brady L Jeannine,
Percival Susan S
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.637.12
Subject(s) - biofilm , streptococcus mutans , thioflavin , chemistry , amyloid (mycology) , microbiology and biotechnology , extracellular polymeric substance , fibril , extracellular , biochemistry , bacteria , biology , alzheimer's disease , disease , inorganic chemistry , genetics , pathology , medicine
Biofilm formation is necessary to establish urinary tract infections, dental caries and numerous other infectious conditions. S. mutans is an organism that forms biofilms and was recently shown to be an amyloid‐forming organism. Amyloids are insoluble fibrillar protein aggregates that have been associated with protein malfolding in disease states such as Alzheimer's, but the concept of functional amyloid formation as a directed process involved in microbial pathogenesis is recently emerging. A panel of well‐characterized cranberry fractions (OSC Inc) was tested to determine if they inhibited S. mutans biofilm formation. The fractions did not affect bacterial growth, but inhibited biofilm formation. As a potential mechanism of biofilm inhibition, amyloid fibrillization by S.mutans extracellular proteins was assessed using a Thioflavin‐T fluorescence assay. Amyloid formation was inhibited by cranberry fractions containing proanthocyanidins. Thus, cranberry bioactive compounds may inhibit biofilm formation by preventing amyloid fibril development of the amyloidogenic proteins produced by S. mutans. Support by Univ Schol Prog, UFL, and NIDCR R01DE21789