Periodate oxidation of R36A pneumococci greatly enhances production of hybridomas secreting anti-protein antibodies

Microb Pathog. 1998 Feb;24(2):111-6. doi: 10.1006/mpat.1997.0175.

Abstract

Most hybridomas derived from mice immunized with non-capsulated Streptococcus pneumoniae strains secrete antibodies to C-polysaccharide epitopes and very rarely against cell wall proteins. Mild periodate oxidation of the non-capsulated R36A pneumococcal strain destroys C-polysaccharide antigenicity without a noticeable loss in the immunizing capacity for proteins. Following immunization of BALB/c mice with periodate-treated R36A cells, most hybridomas obtained (87.5%) secreted anti-pneumococcal protein antibodies. This strategy can be exploited for the development of MAb to pneumococcal polypeptides which, in turn, will be of use in the analysis of pneumococcal cell wall protein antigens.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Bacterial / biosynthesis
  • Antibodies, Bacterial / immunology*
  • Antibodies, Monoclonal / biosynthesis
  • Antibodies, Monoclonal / immunology*
  • Antibody Specificity
  • Bacterial Capsules / chemistry
  • Bacterial Capsules / immunology
  • Bacterial Proteins / immunology*
  • Cell Wall / immunology
  • Epitopes
  • Female
  • Humans
  • Hybridomas / immunology*
  • Immunization
  • Mice
  • Mice, Inbred BALB C
  • Oxidation-Reduction
  • Periodic Acid / pharmacology*
  • Streptococcus pneumoniae / drug effects
  • Streptococcus pneumoniae / immunology*

Substances

  • Antibodies, Bacterial
  • Antibodies, Monoclonal
  • Bacterial Proteins
  • Epitopes
  • Periodic Acid
  • metaperiodate