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The gIII gene located in U region of Yangsan strain, a field isolate of Aujeszkys disease virus (ADV) in Korea, was cloned into pTZ18R and sequenced. The glll gene consisting of 1,437 nucleotides showed 98 % sequence homology with that of Becker strain, a reference strain of ADV. The gene encoding gK of Yangsan strain was placed under the control of Autographa californica nucleopolyhedrosis virus (AcNPV) polyhedrin promoter, and expressed by the derived recombinant baculovirus using Spodoptera frugiperda 9 (Sf9) cells. The expressed g Ill was a protein with molecular weight of 72kd determined by immunoprecipitation and Western blotting assay using anti-ADV polyclonal antibodies and anti-g IE monoclonal antibody. The partially purified g lll protein was utilized as antigen in the radial immunodiffusion enzyme assay (RIDEA) to detect the specific antibody against ADV in pig sera. The results indicated that the sensitivity of RIDEA with the recombinant gIll protein antigen (98% ) was as high as that with the conventional glycoprotein antigen extracted from the ADV infected cells. In addition, the false positive and false negative reactions in gIE RIDEA were significantly reduced than the conventional glycoprotein RIDEA as judged from the results of standard serum neutralization test.

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