BrkA is a Bvg-regulated Bordetella pertussis protein that mediates serum re
sistance and adherence. It shares sequence identity with another B. pertuss
is virulence factor called pertactin, and it is a member of the diverse gro
up of proteins found in Gram-negative bacteria that are secreted by an auto
transporter mechanism. Sera, either from individuals who have been vaccinat
ed with acellular pertussis vaccines, or from individuals who have no re-co
llection of recent infection with B. pertussis fail to kill wild-type B. pe
rtussis, but kill brkA mutant strains very well. We examined whether BrkA c
ould be neutralised in serum fitting this profile. BrkA is synthesised as a
103 kDa precursor that is processed into a surface-associated N-terminal 7
3 kDa passenger domain, and an outer-membrane embedded C-terminal 30 kDa tr
ansporter moiety. Polyclonal antibodies were raised to a recombinant, re-fo
lded histidine-tagged fusion protein representing the 73 kDa passenger regi
on. These anti-BrkA antibodies were shown to boost the existing bactericida
l capacity of human serum against B. Pertussis by neutralising BrkA. (C) 20
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