Analysis of the human Ig isotype response to lactoferrin binding protein A from Neisseria meningitidis

Alison S. Johnson*, Andrew Gorringe, Fiona G. Mackinnon, Andrew J. Fox, Raymond Borrow, Andrew Robinson

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

14 Citations (Scopus)


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. Copyright (C) 1999 Federation of European Microbiological Societies.

Original languageEnglish
Pages (from-to)349-354
Number of pages6
JournalFEMS Immunology and Medical Microbiology
Issue number4
Publication statusPublished - Sep 1999

Bibliographical note

Funding Information:
The authors would like to thank Dr Tony Swan at the PHLS Statistics Unit, Communicable Disease Surveillance Centre, Colindale for statistical support. The work at CAMR was supported by the UK Department of Health.


  • Immune response
  • Lactoferrin binding protein
  • Meningococcal vaccine
  • Neisseria meningitidis


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