Open AccessAnalysis of the human Ig isotype response to lactoferrin binding protein A from Neisseria meningitidis
Author(s) -
Johnson Alison S.,
Gorringe Andrew R.,
Mackin Fiona G.,
Fox Andrew J.,
Borrow Ray,
Robinson Andrew
Publication year - 1999
Publication title -
fems immunology & medical microbiology
Language(s) - English
Resource type - Journals
eISSN - 1574-695X
pISSN - 0928-8244
DOI - 10.1111/j.1574-695x.1999.tb01359.x
Subject(s) - lactoferrin , neisseria meningitidis , biology , antigen , transferrin , antibody , microbiology and biotechnology , neisseriaceae , iron binding proteins , isotype , immunogenicity , ovotransferrin , meningococcal vaccine , immunoglobulin g , virology , immunology , monoclonal antibody , bacteria , immunization , biochemistry , antibiotics , genetics
An effective vaccine for serogroup B meningococci has yet to be developed and attention has turned to subcapsular antigens of the meningococcus as possible vaccine candidates. Iron binding proteins are being studied, with most interest focused on the transferrin binding proteins (TbpA and TbpB) and the ferric binding protein (FbpA). This study describes the purification of lactoferrin binding protein A (LbpA) from two meningococcal strains and assesses the human isotype‐specific serum antibody response to these proteins in patients with proven meningococcal disease due to a range of phenotypes. Overall, fewer than 50% of sera contained IgG that recognised LbpA isolated from either strain and this antibody response was not uniform between the two proteins. There was some evidence that the antibody response varied between meningococcal phenotypes. This study demonstrates that LbpA does not induce a highly cross‐reactive antibody response, indicating that it is unlikely to be an effective vaccine antigen.