期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1986
卷号：83
期号：24
页码：9709-9713
DOI：10.1073/pnas.83.24.9709
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：By analogy to other retroviruses, the major envelope glycoprotein, gp120, of human T-lymphotropic virus type III (HTLV-III) is a probable target for neutralizing antibody. This antigen has been purified from H9 cells chronically infected with the HTLV-IIIB prototype strain. Several goats immunized with the gp120 produced antibodies that neutralized infection of H9 cells by the homologous virus isolate. These same sera failed to neutralize the divergent HTLV-IIIRF isolate. Individuals infected with HTLV-III commonly develop antibodies to gp120 that could be isolated by using the gp120 antigen coupled to an immunoadsorbent resin. The antibody fraction that bound tightly to such a resin was found to neutralize the IIIB but not the RF isolate in a similar fashion as the goat anti-gp120 sera. However, the nonbinding fraction (effluent) from the resin also contained neutralizing activity that was able to block infection by both virus isolates with similar efficacy. Human antibodies to the other virus envelope gene product, the transmembrane gp41, were also affinity purified by utilizing the recombinant peptide 121, but these failed to influence infection by either virus isolate.
