Synthetic peptide segments from Escherichia coli porin OmpF constitute leukocyte activators

H. M. Vordermeier, P. Hoffmann, F. O. Gombert, G. Jung, W. G. Bessler*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

After characterization of the porin OmpF and selection of molecular structures responsible for leukocyte activation by using computer-assisted epitope analysis, the analogs OmpF (153-174) (containing amino acids 153 to 174), OmpF (157-174), and OmpF (275-284) were synthesized and tested. Like the native protein, the segments were mitogenic for BALB/c splenocytes and induced B lymphocyte differentiation into antibody-producing plasma cells and tumor cytotoxicity of macrophages against the fibroblast cell line L929. We thus demonstrated that defined peptide segments are responsible for the leukocyte-activating properties of a major bacterial surface protein.

Original languageEnglish
Pages (from-to)2719-2724
Number of pages6
JournalInfection and Immunity
Volume58
Issue number8
DOIs
Publication statusPublished - 01 Aug 1990

Keywords

  • Animals
  • B-Lymphocytes/immunology
  • Bacterial Outer Membrane Proteins/chemical synthesis
  • Bone Marrow/immunology
  • Epitopes
  • Escherichia coli/immunology
  • Lymphocyte Activation/immunology
  • Macrophages/immunology
  • Mice
  • Mice, Inbred BALB C
  • Mice, Inbred C3H
  • Peptides/chemical synthesis
  • Porins
  • Spleen/immunology
  • Tumor Cells, Cultured

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