Decorinbinding

Decorin-binding refers to molecular interactions that involve decorin, a small leucine-rich proteoglycan of the extracellular matrix. Decorin binds to collagen type I and other ECM components, and it modulates tissue architecture and cell signaling by interacting with cell surface receptors and growth factors such as TGF-β. Through these interactions, decorin influences collagen fibrillogenesis, ECM organization, and cellular responses to injury and inflammation.

In microbiology, decorin-binding describes the ability of certain pathogens to adhere to host tissues by binding decorin. The best-characterized example is Borrelia burgdorferi, the bacterium that causes Lyme disease, which expresses decorin-binding proteins DbpA and DbpB on its surface. These outer-surface lipoproteins bind decorin, promoting adherence to decorin-rich tissues and facilitating colonization and dissemination to sites such as skin, joints, and nervous tissue. Expression of DbpA/DbpB varies among Borrelia strains and can influence tissue tropism and virulence.

Clinical and research relevance includes the study of decorin-binding interactions as potential targets for interventions that block bacterial adhesion. Beyond pathogen interactions, decorin’s binding activities with collagen and receptors play a central role in normal ECM biology, tissue remodeling, and signaling processes.