PorB3 outer membrane protein on Neisseria meningitidis is poorly accessible for antibody binding on live bacteria

Vaccine. 2001 Jan 8;19(11-12):1526-33. doi: 10.1016/s0264-410x(00)00324-8.


It is reported here that the PorB3 porin proteins of serotype 4 and 15 are poorly accessible for antibody binding on live Neisseria meningitidis bacteria, whereas the allelic PorB2 and the PorA outer membrane protein appear to be highly accessible. This was revealed by flow cytometry analysis using several mouse monoclonal antibodies (mAbs) as well as PorB3 specific antibodies isolated from post vaccination and patient sera. However, strong antibody binding to the PorB3 protein was observed after killing the bacteria with ethanol. The reason for the lack of epitope exposure could be a shielding effect of the carbohydrate chains of lipopolysaccharides (LPS) possibly combined with short extra-cellular loops in the PorB3 protein. The findings indicate that the PorB3 protein is not an optimal target for protective antibodies induced by vaccination.

MeSH terms

  • Animals
  • Antibodies, Bacterial / metabolism*
  • Antibodies, Monoclonal / metabolism
  • Bacterial Outer Membrane Proteins / chemistry
  • Bacterial Outer Membrane Proteins / immunology*
  • Epitopes / chemistry
  • Epitopes / metabolism
  • Humans
  • In Vitro Techniques
  • Lipopolysaccharides / chemistry
  • Lipopolysaccharides / metabolism
  • Meningococcal Infections / immunology
  • Meningococcal Infections / prevention & control
  • Meningococcal Vaccines / immunology
  • Meningococcal Vaccines / pharmacology
  • Mice
  • Neisseria meningitidis / immunology*
  • Porins*
  • Vaccines, Inactivated / immunology
  • Vaccines, Inactivated / pharmacology


  • Antibodies, Bacterial
  • Antibodies, Monoclonal
  • Bacterial Outer Membrane Proteins
  • Epitopes
  • Lipopolysaccharides
  • Meningococcal Vaccines
  • Porins
  • Vaccines, Inactivated
  • porin protein, Neisseria