| Description | Bordetella pertussis is a Gram-negative, aerobic coccobacillus that causes pertussis (whooping cough), especially in young children [ ]. Once present in the lungs, the bacterium attaches to ciliated pulmonary epithelial cells via a collection of outer membrane proteins, all of which are virulence factors.Pertactin, or P69 protein, is one of these virulence factors. Pertactin and filamentous haemagglutinin have been identified as Bordetella adhesins [ ]. Both proteins contain an arg-gly-asp (RGD) motif that promotes binding to integrins, known to be important in cell mobility and development. The production of most Bordetella virulence factors (including pertactin) is controlled by a two-component signal transduction system, comprising the BvgA regulator and the BvgS sensor []. Pertactin shares a high level of similarity with other Bordetella adhesins, such as BrkA. The protein is first produced as a 93kDa precursor. Upon secretion into the extracellular environment, a 30kDa domain at the C terminus remains in the outer membrane, while the mature 60.4kDa pertactin molecule is released [].The crystal structure of mature pertactin has been determined to 2.5A resolution by means of X-ray diffraction. The fold is characterised by a 16-stranded parallel β-helix, with a V-shaped cross-section. Several between-strand amino-acid repeats form internal and external ladders. The helical structure is interrupted by several protruding loops that contain motifs associated with the activity of the protein. One such sequence -[GGXXP]5 -appears directly after the RGD motif, and may mediate interaction with epithelial cells. The C-terminal region of P.69 pertactin contains a [PQP]5 motif loop, which contains the major immunoprotective epitope [ ].The superfamily also includes immunoglobulin A1 protease and adhesion penetration protein HAP. | Name | Pertactin, central region |
| Short Name | Pertactin_central | Type | Domain |
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