Campylobacter coli surface receptors

Campylobacter coli surface receptors are a heterogeneous group of proteins and glycoconjugates located on the outer membrane of the Gram-negative bacterium Campylobacter coli. These molecules serve as the primary interface for interaction with the host environment and are essential for the pathogen's virulence and survival. Key receptors include adhesins such as CadF (Campylobacter adhesion to fibronectin) and FlpA (Fibronectin-like protein A), which mediate binding to host extracellular matrix components to facilitate colonization (Konkel et al., 1997; Flanagan et al., 2009). Additionally, the Major Outer Membrane Protein (MOMP) acts as a porin for nutrient acquisition, while other surface components like PEB1 are involved in both transport and adherence (Bolton, 2015). These receptors are significant targets for the development of vaccines and phage therapies aimed at preventing campylobacteriosis, a leading cause of bacterial gastroenteritis worldwide (Meunier et al., 2016). However, the high degree of phase variation and genetic diversity among C. coli surface proteins presents a challenge for broad-spectrum therapeutic efficacy and may contribute to immune evasion. Furthermore, certain surface structures, such as lipooligosaccharides, can exhibit molecular mimicry with host tissues, potentially triggering autoimmune conditions like Guillain-Barré syndrome (Yuki et al., 2004).

Other names

Campylobacter coli surface proteinsC. coli outer membrane proteinsC. coli adhesinsC. coli surface antigens

Inhibition of bacterial attachment to host intestinal cells, neutralization of virulence factors by specific antibodies, and targeted bacterial lysis via phage binding to surface receptors.