Abstract
A new generation of whooping-cough vaccines contain P.69 pertactin, a surface-exposed domain of an outer membrane protein expressed by the virulent bacterium Bordetella pertussis. This protein is a virulence factor that mediates adhesion to target mammalian cells, a reaction that is in part mediated by an RGD sequence. The X-ray crystal structure of P.69 pertactin has been determined to 2.5 A. The protein fold consists of a 16-stranded parallel beta-helix with a V-shaped cross-section, and is the largest beta-helix known to date. Several between-strand weakly conserved amino-acid repeats form internal and external ladders. The structure appears as a helix from which several loops protrude, which contain sequence motifs associated with the biological activity of the protein. One particular (GGXXP)5 sequence is located directly after the RGD motif, and may mediate interaction with epithelial cells. The carboxy-terminal region of P.69 pertactin incorporates a (PQP)5 motif loop containing the major immunoprotective epitope.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
