| Type: | Family | Name: | Pertactin |
| Description: | Bordetella pertussisis 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. Theproduction of most Bordetella virulence factors (including pertactin) is controlled by a two-component signal transduction system, comprising theBvgA regulator and the BvgS sensor []. Pertactin shares a high level of similarity with other Bordetella adhesins, such as BrkA. The protein isfirst 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 beta-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 []. This entry is the N-terminal end of pertactin and is found associated with the C-terminal section . | Short Name: | Pertactin |
