Amyloid Aggregation of Streptococcus mutans Cnm Influences Its Collagen-Binding Activity
Nicholas de Mojana di Cologna, Sandip Samaddar, Carolina A. Valle, Jonathan Vargas, Alejandro Avilés-Reyes, J. C. Tabares Morales, Tridib Ganguly, Roberta Pileggi, L. Jeannine Brady, José A. Lemos, Jacqueline Abranches
Abstract
Streptococcus mutans is a keystone pathogen that promotes caries by acidifying the dental biofilm milieu. The collagen- and laminin-binding glycoprotein Cnm is a virulence factor of S. mutans. Expression of Cnm by S. mutans is hypothesized to contribute to niche expansion, allowing colonization of multiple sites in the body, including collagen-rich surfaces such as dentin and heart valves. Here, we suggest that Cnm function might be modulated by its aggregation status. As a monomer, its primary function is to promote attachment to collagenous substrates via its collagen-binding domain (CBD). However, in later stages of biofilm maturation, the same CBD of Cnm could self-assemble into amyloid fibrils, losing the ability to bind to collagen and likely becoming a component of the biofilm matrix. Our findings shed light on the role of functional amyloids in S. mutans pathobiology and ecology.