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

FEMS Immunol Med Microbiol. 1999 Sep;25(4):349-54. doi: 10.1111/j.1574-695X.1999.tb01359.x.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Bacterial / blood
  • Antibodies, Bacterial / classification
  • Antibodies, Bacterial / immunology*
  • Bacterial Outer Membrane Proteins / immunology*
  • Bacterial Outer Membrane Proteins / metabolism
  • Humans
  • Immunoglobulin Isotypes*
  • Lactoferrin / metabolism*
  • Meningococcal Infections / blood
  • Meningococcal Infections / immunology*
  • Neisseria meningitidis / immunology*
  • Receptors, Cell Surface / immunology*
  • Receptors, Cell Surface / metabolism

Substances

  • Antibodies, Bacterial
  • Bacterial Outer Membrane Proteins
  • Immunoglobulin Isotypes
  • LBPA protein, Neisseria meningitidis
  • Receptors, Cell Surface
  • Lactoferrin