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Bordetella pertussis surface and secreted antigens are a group of specialized proteins that facilitate the colonization and pathogenesis of the bacterium responsible for whooping cough. Key components include pertussis toxin (PT), filamentous hemagglutinin (FHA), pertactin (PRN), and fimbriae (Fim2 and Fim3) [Source: CDC]. Pertussis toxin is a major virulence factor that enters host cells and ADP-ribosylates inhibitory G proteins, leading to deregulated cAMP signaling and immune cell dysfunction [Source: PubMed, PMID: 25135706]. FHA and fimbriae are critical adhesins that allow the bacteria to bind to the ciliated respiratory epithelium, while PRN aids in attachment and resistance to host clearance [Source: UniProt, P04977]. These antigens serve as the primary targets for acellular pertussis (aP) vaccines, which aim to induce high titers of neutralizing antibodies [Source: NIH]. While effective at preventing severe disease, these targets face challenges such as the rapid waning of antibody-mediated protection compared to whole-cell vaccines [Source: PubMed, PMID: 29445124]. Additionally, the emergence of PRN-deficient strains suggests that the bacterium is evolving in response to vaccine-induced selective pressure [Source: PubMed, PMID: 24332841].
Active immunization to elicit neutralizing antibodies that inhibit bacterial attachment and neutralize exotoxins.
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