The filamentous hemagglutinin (FHA) of Bordetella pertussis is a principal
adhesin, which plays a key role in the colonization of the upper respirator
y tract. FHA is also a protective antigen, which has been incorporated in t
he new generation of acellular vaccines against whooping cough. The protein
is synthesized as a large 367-kDa precursor, which is then processed into
a 220-kDa secreted polypeptide. To optimize the use of this protein for vac
cine purposes it would be helpful to define the regions encompassing immuno
dominant epitopes. Twelve recombinant plasmids have been generated encoding
fusion proteins between fragments of the matured-secreted 220-kDa form of
FHA and the vector-encoded phage MS2 polymerase. Protein extracts of the re
sulting; recombinant clones have been tested for reactivity with sera from
20 patients convalescent from whooping cough, and two human standard sera.
The results indicate the presence of an immunodominant B cell epitope in th
e polypeptide coded by a I-kb DNA fragment encompassing positions 5781-6800
of the published sequence. These results suggest that the identified fragm
ent should be conserved in the formulation of vaccines against pertussis. (
C) 1999 Federation of European Microbiological Societies. Published by Else
vier Science B.V. All rights reserved.