Abstract
The binding of monoclonal antibodies obtained after immunization with tobacco mosaic protein was analyzed by electron microscopy. A method was developed for visualizing the viral antigen reacting in different ELISA procedures. It was found that the use of a pH 9.6 buffer during the coating of ELISA plates led to the dissociation of virions into subunits which bound preferentially to the solid phase. MAbs that reacted with both virions and subunits in ELISA were found to bind to one of the two extremities of viral rods. These MAbs also reacted with viral protein aggregated in the form of disks. In contrast, MAbs reacting only with virions in ELISA were found to bind over the entire surface of the virus.
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