Antigenic specificity of Escherichia coli alkaline phosphatase studied with monoclonal antibodies: Immunological characterization of E. coli and Shigella strains |
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| Affiliation: | 1. Department of Kinesiology, Iowa State University, Forker Building, Ames, Iowa, USA;2. School of Kinesiology and Recreation, Illinois State University, McCormick Hall, Normal, Illinois, USA;1. School of Laboratory Medicine and Life Science/Institute of Biomedical Informatics, Wenzhou Medical University, Wenzhou 325035, China;2. The Second Affiliated Hospital, Wenzhou Medical University, Wenzhou 325000, China;3. 118 Hospital of PLA, Wenzhou 325000, China;4. Institute of Hydrobiology, The Chinese Academy of Sciences, Wuhan, China;5. University of Chinese Academy of Sciences, Beijing, China |
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| Abstract: | Monoclonal antibodies (MoAb) to the alkaline phosphatase of Escherichia coli were produced from spleen cells of BALB/c mice primed with purified alkaline phosphatase of E. coli and SP2O/Ag-14 myeloma cells. Five stable clones were established. They all produced antibodies which reacted by enzyme-linked immunosorbent assay (ELISA) with alkaline phosphatase of all E. coli (25 strains) independently of their origin (drinking water, saline water, surface water, faecal or clinical origin), and with that of four Shigella species (7 strains) tested. Four of these MoAb gave a positive reaction with 52 % (MoAb 4G10), 73 % (MoAb 4F8, MoAb 4G6) and 89 % (MoAb 3C8) of 14 other bacterial species (30 strains) studied, while one (MoAb 2E5) did not react with alkaline phosphatase of these unrelated bacterial strains and thus appeared specific for E. coli and Shigella species. This MoAb was still detectable in ascitic fluids at 1/500,000 in ELISA, and detected all E. coli strains in an indirect immunofluorescence assay at 1/100. It could therefore be used as a reagent for routine detection of E. coli in drinking water, food or clinical specimens. |
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