The recombinant protein (r1448) in crude lysate of insect cells infected with a previously devcl-oped recombinant baculovirus, expressing two structural protcins, the nucleocapsid protein (p14) and the envelope glycoprotein (gp48) of the NADL strain of bovine viral diarrhea virus (BVDV), was evaluated as a coating antigen in a Standard enzyme-linked immunosorbent assay (ELISA) for detection of antibody against homol- ogous and heterologous strains of BVDV. The ELISA was compared to standard virus neutrali-zation test (VNT) for detection of antibody against the local Iman strain of BVDV in sera of calves immunized with the locally produced Pneumo-3 inactivated vaccine, experimentally in- fected calves and contact controls. Antibody titers  With ELISA were closcly corrclatcd ‘ibody titers estimated by VNT (averager= 0.917). Nevertheless, thc recombinant protcin (r1448) was an effective and inexpensive ELISA antigen for detection of antibody against homolo- gous and heterologous strains of both gcnotypcs of BVDV (BVDVI and BVDV2) In reference hyperimmune cattle scra. In conclusion, the recombinant antigen (r1448) is a reliable candi-date for diagnostic tests of BVDV infections in Egypt.