PJB-2008-90
PURIFICATION AND PROTECTIVE EFFICACY OF RE-NATURED C-TERMINAL DOMAIN (P.30) OF PERTACTIN AUTOTRANSPORTER PROTEIN OF BORDETELLA PERTUSSIS
S. HABIB BOKHARI1* AND P. BLACKBURN2
Abstract
Members of the Bordetella pertussis autotransporter family are grouped together on the basis of homology at their C-termini. The full pathogenic potential of the B. pertussis is partly contributed by the members of its autotransporter family, which are usually either exported to the bacterial cell surface or secreted into the external environment. The β-barrel (C-terminus) forming domain plays a key role in surface localization of the virulence associated passenger domains of autotransporter proteins. The protective capacity of the C-terminus (P.30) of B. pertussis autotransporter protein pertactin was studied in mouse protection studies.
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