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Southern Bean Mosaic Virus Monoclonal Antibodies: Reactivity with Virus Strains and with the Virus Antigen in Different Conformations. J. H. Tremaine, Research scientist, Agriculture Canada, Research Station, 6660 N.W. Marine Drive, Vancouver, British Columbia, Canada V6T 1X2; W. P. Ronald(2), and D. J. MacKenzie(3). (2)(3)Technicians, respectively, Agriculture Canada, Research Station, 6660 N.W. Marine Drive, Vancouver, British Columbia, Canada V6T 1X2. Phytopathology 75:1208-1212. Accepted for publication 12 June 1985. Copyright 1985 Department of Agriculture, Government of Canada. DOI: 10.1094/Phyto-75-1208.

Monoclonal antibodies B4 to B10 were produced against southern bean mosaic virus bean-type strain and C1 and C3 against the cowpea-type strain. They were tested against virus, swollen virus, and virus protein antigens from five bean strains and four cowpea strains in gel diffusion, immunoelectron microscopy, indirect enzyme-linked immunosorbent assay (ELISA), double antibody sandwich (DAS)-ELISA, antigen competition ELISA, and latex agglutination tests. B5, B6, and B10 were predominantly virus reactors with bean strains only. They precipitated virus, but not swollen virus and protein, in gel diffusion and immunoelectron microscopy; they reacted well with virus in indirect ELISA, but B6 and B10 had lower reactivities with protein and with swollen virus and protein, respectively. B4, B7, B8, B9, C1, and C3 were predominantly swollen virus and protein reactors with both bean and cowpea strains. They did not react with virus, swollen virus, or protein in gel diffusion or immunoelectron microscopy but reacted with swollen virus and protein and weakly with virus in indirect ELISA. B7 and C1 reacted strongly with virus in DAS-ELISA and B7 reacted with virus in latex agglutination tests. However, B7 and B9 were inhibited by swollen virus and protein but not by virus in competitive inhibition assays. The reaction of these antibodies with virus in indirect ELISA, latex agglutination tests, and DAS-ELISA was attributed to denaturation of virus on polystyrene plates and latex beads or by reaction with polyclonal antibodies in DAS-ELISA. The binding sites of B5, B6, and B10 on the virion of the bean-type strain were not blocked by the reaction of the virus with trinitrobenzenesulfonic acid.