Amyloid Aggregation of Streptococcus mutans Cnm Influences Its Collagen-Binding Activity.

ABSTRACT: The cnm gene, coding for the glycosylated collagen- and laminin-binding surface adhesin Cnm, is found in the genomes of approximately 20% of Streptococcus mutans clinical isolates and is associated with systemic infections and increased caries risk. Other surface-associated collagen-binding proteins of S. mutans, such as P1 and WapA, have been demonstrated to form an amyloid quaternary structure with functional implications within biofilms. In silico analysis predicted that the β-sheet-rich N-terminal collagen-binding domain (CBD) of Cnm has a propensity for amyloid aggregation, whereas the threonine-rich C-terminal domain was predicted to be disorganized. In this study, thioflavin-T fluorescence and electron microscopy were used to show that Cnm forms amyloids in either its

SUBMITTER: di Cologna NM 

PROVIDER: S-EPMC8516039 | biostudies-literature | 2021 Oct

REPOSITORIES: biostudies-literature