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 language | English |
---|---|
Pages (from-to) | 2719-2724 |
Number of pages | 6 |
Journal | Infection and Immunity |
Volume | 58 |
Issue number | 8 |
DOIs | |
Publication status | Published - 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