IgA1 antibodies specific for outer membrane protein PorA modulate the interaction between Neisseria meningitidis and the epithelium

Microb Pathog. 2009 May;46(5):253-60. doi: 10.1016/j.micpath.2009.01.009. Epub 2009 Feb 5.

Abstract

Despite high carriage rates of Neisseria meningitidis, incidence of meningococcal disease remains low, partially due to development of natural immunity. We have previously demonstrated an inverse relationship between salivary anti-meningococcal IgA and disease incidence, but little is known about the contribution of IgA to immunity at mucosal surfaces. Here we show strong immunoreactivity by human salivary IgA against the meningococcal outer membrane porin, PorA. Monomeric anti-PorA IgA1 (humanized chimeric antibodies) but not IgG increased the association of unencapsulated serogroup B N. meningitidis (H44/76) with Chang (conjunctival) but not with either Detroit (pharyngeal) cells or with A549 (alveolar) epithelial cells. Association of encapsulated N. meningitidis was not increased. Epithelial binding of IgA was Fc fragment dependent and not inhibited by IgM. Together these data suggest the presence of a specific epithelial IgA receptor that could influence the effect of both naturally acquired and vaccine induced IgA antibodies at the epithelial surface.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibodies, Bacterial / immunology
  • Cell Line
  • Epithelium / immunology*
  • Epithelium / microbiology
  • Host-Pathogen Interactions*
  • Humans
  • Immunoglobulin A / immunology*
  • Immunoglobulin G / immunology
  • Meningococcal Infections / immunology*
  • Meningococcal Infections / microbiology
  • Neisseria meningitidis / immunology*
  • Porins / immunology*

Substances

  • Antibodies, Bacterial
  • Immunoglobulin A
  • Immunoglobulin G
  • Porins
  • porin protein, Neisseria