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Campylobacter jejuni surface antigens comprise a diverse array of molecules, including proteins and lipooligosaccharides (LOS), that are exposed on the bacterial exterior and are vital for host-pathogen interactions. Key antigenic components include the flagellar proteins (FlaA and FlaB), the major outer membrane protein (MOMP), and various adhesins such as CadF and Peb1, which facilitate bacterial motility through the intestinal mucus and attachment to epithelial cells (Poly & Guerry, 2008). These antigens are the primary targets of the host immune system during campylobacteriosis, the leading cause of bacterial foodborne gastroenteritis worldwide (Young et al., 2007). A critical clinical aspect of these antigens is the presence of sialylated LOS structures that can mimic human gangliosides, potentially triggering the autoimmune peripheral neuropathy known as Guillain-Barré syndrome (Yuki, 2001). Therapeutic strategies targeting these antigens primarily focus on vaccine development and passive immunization to prevent colonization, though researchers must carefully navigate the risks of molecular mimicry to ensure safety (Riddle et al., 2012).
Induction of neutralizing mucosal and systemic antibodies (IgA and IgG) to inhibit bacterial motility, adherence, and colonization of the intestinal epithelium.
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