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Monoclonal antibodies against two of the proteins specified by one of the transforming genes (early region 1 B) of human adenovirus type 2 have been produced and characterized. Two clones (RAl and PA6), generated by fusion of mouse myeloma NSO cells with splenocytes from rats immunized with whole-cell lysates of an adenovirus-transformed rat cell line (F 19), secreted antibodies against a 58 kDa protein. Another clone (DC1) produced antibodies against the same protein, and resulted from fusion of immune rat splenocytes with the rat myeloma Y3.Ag.1.2.3. Immunoprecipitation studies showed that all three antibodies recognized [35S]-methionine-labelled 58kDa protein, and phosphorylated derivatives of the 58kDa protein labelled with [32P]orthophosphate present in infected human cells. One clone (EC3) produced antibody against a l9kDa protein also encoded by early region 1 B, but not sharing sequence homology with 58 kDa. The identity of the 19 kDa protein recognized by the EC3 antibody was established by immunoprecipitation from lysates of labelled-infected cells and from products of cell-free translation directed by mRNA isolated from adenovirus 2-infected cells. Indirect immunofluorescentantibody staining of infected human cells using the RAI and EC3 antibodies revealed a nuclear location of the 58 kDa protein and a mainly cytoplasmic location of the l9kDa protein.

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