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Campylobacter jejuni and Campylobacter coli whole-cell surface antigens encompass a diverse group of molecules, including flagellin (FlaA), major outer membrane proteins (MOMP), and lipooligosaccharides (LOS), which are essential for the bacteria's survival and pathogenicity (Zhang et al., 2020, Frontiers in Microbiology). These antigens facilitate critical processes such as motility, adherence to the intestinal mucosa, and colonization of the host gut (CDC, 2022). As the primary interface between the pathogen and the host, they are the focus of intense research for vaccine development and diagnostic assays (Meunier et al., 2016, Vaccine). In clinical settings, these antigens are responsible for triggering campylobacteriosis, one of the most common causes of bacterial foodborne illness worldwide (WHO, 2020). A major therapeutic challenge associated with these antigens is the potential for molecular mimicry, where certain LOS structures resemble human gangliosides, leading to the production of autoantibodies and the subsequent development of Guillain-Barré syndrome (Yuki et al., 2004, Journal of Infectious Diseases). Consequently, vaccine strategies often aim to utilize specific, non-mimicking protein subunits rather than whole-cell preparations to ensure safety.
Induction of active immunity through the presentation of bacterial epitopes to B and T cells, leading to the production of neutralizing antibodies (IgA and IgG) that inhibit bacterial adhesion and colonization (Meunier et al., 2016, Vaccine).
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