Functional Analysis of the Collagen Binding Proteins of Streptococcus parasanguinis FW213

Abstract

Bacteria generally can utilize multiple adhesins to establish themselves in the host. We found that Streptococcus parasanguinis , a dominant oral commensal and an opportunistic pathogen for subacute endocarditis, possesses at least three collagen-binding proteins that enable S. parasanguinis to successfully colonize damaged heart tissues and escape innate immune clearance. The binding specificities of these three proteins for extracellular matrix molecules differ, although all three proteins participate in biofilm formation by S. parasanguinis . The “multiligand for multisubstrate” feature of these adhesins may explain the high adaptability of this microbe to different tissue sites.