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  • Author or Editor: Angeles Morales x
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Hybridomas secreting monoclonal antibodies (mab) to transmissible gastroenteritis virus (tgev) were produced by fusion of SP2/0 myeloma cells and splenic lymphocytes of BALB/c mice immunized with the virulent cell-passaged Miller strain of tgev. The mab secreted by these hybridomas were partially characterized; 4 of them (MA4, MA5, MH11, MB2) had high-neutralization titer for tgev. The remaining 7 (MC6, MD9, ME5, MG5, MF2, ME9, MG7) did not neutralize tgev at 1:25 dilution. All 4 neutralizing and 2 of the nonneutralizing mab reacted with the E2 protein of tgev in a radioimmunoprecipitation assay. The remaining 5 mab reacted with the E1 protein of tgev. Reactivity of the mab was tested in an indirect immunofluorescent assay with 3 cell culture-adapted strains of tgev (Miller, Purdue, and Illinois) and 13 wild-type isolates of tgev. Neutralizing mab reacted with all 13 wild-type isolates and the 3 cell culture-adapted strains of tgev. In contrast, nonneutralizing mab that reacted with the Miller strain of TGEV varied in their reactivity with the wild-type tgev isolates. Reactivity of neutralizing mab was also tested, using plaque-reduction neutralization assays with Miller, Purdue, and Illinois strains and 5 wild-type isolates. All 4 neutralizing mab neutralized the 8 virus isolates, but the neutralization titer was higher with the homologous virus than with the heterologous virus isolates. However, neutralization titers of the 4 neutralizing mab were 4 to 16 times higher for the homologous Miller strain of tgev than for the heterologous Illinois and Purdue strains, and were 4 to 1,000 times higher than for the wild-type isolates. Extensive antigenic heterogeneity was observed among tgev isolates on epitopes recognized by the nonneutralizing mab directed against either E1 or E2 protein.

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in American Journal of Veterinary Research