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 pertussis1–3. This protein is a virulence factor that mediates adhesion to target mammalian cells, a reaction that is in part mediated by an RGB sequence. The X-ray crystal structure of P.69 pertactin has been determined to 2.5 Å. The protein fold consists of a 16-stranded parallel β-helix with a V-shaped cross-section, and is the largest β-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 RGB 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.
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Emsley, P., Charles, I., Fairweather, N. et al. Structure of Bordetella pertussis virulence factor P.69 pertactin. Nature 381, 90–92 (1996). https://doi.org/10.1038/381090a0
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DOI: https://doi.org/10.1038/381090a0
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