Clostridioides difficile surface layer protein A (SlpA) (SlpA)

Clostridioides difficile (formerly Clostridium difficile) bacterial cell surface receptors, primarily represented by the Surface Layer Protein A (SlpA) and a family of associated Cell Wall Proteins (CWPs), are critical structural and functional components of the bacterial envelope. SlpA is the most abundant protein on the vegetative cell surface, where it assembles into a paracrystalline S-layer that provides structural integrity and serves as a major adhesin for binding to the host's intestinal epithelium. These surface proteins are essential for the initial stages of colonization, biofilm formation, and the regulation of toxin secretion (TcdA and TcdB), which are the primary drivers of C. difficile infection (CDI) pathogenesis. Additionally, SlpA acts as a primary receptor for many C. difficile-specific bacteriophages and R-type bacteriocins, making it a high-priority target for narrow-spectrum therapeutic interventions. Targeting these receptors with monoclonal antibodies, vaccines, or phage-based therapies aims to prevent bacterial adhesion and colonization, thereby reducing the incidence and recurrence of CDI while preserving the protective gut microbiota.

Other names

Surface layer protein AS-layer proteinCell wall protein (CWP)SlpA precursorHigh-molecular-weight surface layer protein (HMW-SLP)Low-molecular-weight surface layer protein (LMW-SLP)Cwp84Cwp66Bacterial adhesinBile salt receptor CspC

Inhibition of bacterial adhesion to host cells, disruption of S-layer assembly, and phage-mediated bacterial lysis to prevent colonization and virulence.