SUMMARYThe reported serological relatedness between the major glycoproteins of human immunodeficiency virus (HIV gpl20) and equine infectious anaemia virus (EIAV gp90) was examined using purified antigens in radioimmunoprecipitation (RIP), radioimmunoassay (RIA) and immunoblot assays with reference serum from acquired immunodeficiency syndrome (AIDS) patients, an anti-gpl20 goat serum and EIAVinfected horse serum. To assess the contributions of glycoprotein oligosaccharide and peptide components to any observed reactivities, antigens treated with endoglycosidase F to remove carbohydrate were assayed in parallel with the intact glycoprotein. The results of the experiments indicated that the reactivity observed for each antigen was dependent on the immunoassay employed. The RIP and RIA analyses demonstrated that HIV gp 120 is equally reactive with the AIDS patient serum, the goat anti-gp 120 serum and the EIAV-infected horse serum, whereas the EIAV gp90 reacted only with the horse serum. In immunoblot assays, the HIV gpl20 reacted with AIDS patient serum, but not with the EIAV-infected horse serum. Deglycosylation of the HIV gpl20 evidently increased its reactivity with the AIDS patient serum, had no significant effect on its reactivity with the goat antiserum, and essentially abolished its reactivity with the EIAV reference serum. Thus, it appears that the serological crossreactivity observed between HIV gpl20 and sera from EIAV-infected horses can be attributed to the oligosaccharide rather than the peptide components of the viral glycoprotein. These studies also emphasize the necessity of employing several assay procedures in assessing lentivirus antigenicity.