Choline-binding protein D (CbpD)

Choline-binding protein D is a modular surface protein found in *Streptococcus pneumoniae* and related bacteria. It binds to choline molecules present on bacterial cell wall teichoic acids through a series of conserved choline-binding repeats (CBRs), organizing into an elongated, superhelical structure. This anchoring allows CbpD to mediate bacterial cell wall remodeling, cell separation, adherence to host tissues, and enhances bacterial virulence during infection. CbpD is thought to play an important role in pneumococcal pathogenesis, making it a potential target for antibacterial drug discovery or novel therapeutic interventions aimed at disrupting pathogenic mechanisms. CbpD consists of distinct domains: an N-terminal signal peptide, a central region often involved in particular interactions, and a C-terminal choline-binding domain assembled from several choline-binding repeats. It is non-enzymatic but can function in concert with autolysins or other enzymes that participate in cell wall turnover. Its loss or mutation can attenuate bacterial virulence and impact colonization, underlining its value as a drug target.

Other names

CBP-DCbpD

Block choline-binding interactions, preventing anchoring to cell wall. Inhibit the protein's contribution to cell separation and virulence.