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Pertactin is a 69 kDa surface-anchored autotransporter protein and a critical virulence factor of Bordetella pertussis, the primary causative agent of whooping cough. It functions as an adhesin, utilizing an Arg-Gly-Asp (RGD) motif to facilitate bacterial attachment to host tracheal epithelial cells and to resist clearance by the host's innate immune system, particularly neutrophils. Due to its high immunogenicity and role in pathogenesis, pertactin is a key subunit antigen included in modern acellular pertussis vaccines (aP), such as DTaP and Tdap. Vaccination with pertactin induces the production of specific antibodies that promote bacterial killing through complement activation and opsonophagocytosis. However, the widespread use of pertactin-containing vaccines has exerted selective pressure on bacterial populations, leading to the global emergence of pertactin-deficient strains. This antigenic divergence represents a significant therapeutic challenge, as it may contribute to reduced vaccine effectiveness and the resurgence of pertussis in highly vaccinated populations.
Induction of neutralizing and bactericidal antibodies that activate the complement pathway (C1q), leading to membrane attack complex (MAC) formation and opsonophagocytosis of Bordetella pertussis.
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