To evaluate the performance of a serological test for human immunodeficiency virus type 1 (HIV-1)
infections based on the use of a recombinant envelope gene-derived
protein as the
antigen, we caused expression of a 1.4-kilobase fragment of HIV.
DNA that codes for the complete gp41 transmembrane
protein in an Escherichia coli expression vector and used Western blots (WB; immunoblots) prepared with recombinant material (pEX-41) to detect
antibodies to HIV-1. This test detected all 339 sera which were positive by a combination of conventional serodiagnostic assays and produced no false-positive results with 311 negative samples. Also no false-positive results were obtained with 20 sera from
systemic lupus erythematosus patients which had high titers of cross-reactive
autoantibodies. In six cases, the pEX-41 WB proved to be more sensitive than individual assays applied on their own, and in five cases it was even more sensitive than a combination of conventional assays. We tested 221 sera in both our pEX-41 WB and a commercially available recombinant
enzyme immunoassay (EIA [Abbott]). The results were identical in 188 cases. A total of 27 sera containing
antibodies to gp41 as demonstrated in the pEX-41 WB, as well as the Abbott recombinant EIA, had no
antibodies to the recombinant core
antigen as measured in the Abbott EIA. However, 25 of these sera did
stain the 24-kilodalton band on a WB with purified virus. Six sera that were positive in all of the conventional confirmatory assays and reacted strongly with the pEX-41 WB did not recognize the
surface antigen used in the Abbott recombinant EIA. We conclude that the use of WB prepared with recombinant-derived p41 offers a very sensitive and specific method to detect
antibodies to HIV.