BBK32 attenuates antibody-dependent complement-mediated killing of infectious Borreliella burgdorferi isolates.

ABSTRACT: Borreliella burgdorferi, the causative agent of Lyme disease, has evolved unique complement evasion proteins that promote its ability to establish and maintain infection in mammalian hosts. Among these is B. burgdorferi BBK32, a multifunctional surface lipoprotein that binds extracellular matrix (ECM) components, including fibronectin (Fn). In addition to its ECM-binding functions, BBK32 binds to C1r, the initiator protease of the classical pathway of complement, and protects B. burgdorferi from complement-mediated killing following exposure to normal human serum. The disparate functions of BBK32 in adhesion and complement evasion have previously been studied in isolation. Herein we demonstrate that full-length BBK32 binds both Fn and C1 concurrently, indicating that binding of these macro

SUBMITTER: Powell-Pierce AD 

PROVIDER: S-EPMC12316396 | biostudies-literature | 2025 Jul

REPOSITORIES: biostudies-literature