ENHANCED ENDOCYTOSIS AND ANTI-HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 ACTIVITY OF ANTI-REV ANTIBODIES AFTER CATIONIZATION

Transmembrane transport and endocytosis of antibodies is facilitated b y cationization, when the isoelectric point of the antibody is raised to the cationic range. The present studies describe the preparation of affinity-purified polyclonal antibodies directed against a 16-amino a cid synthetic peptide corresponding to amino acids 35-50 of the 116-am ino acid rev protein of human immunodeficiency virus type 1 (HIV-1). T he concentration of cationized anti-rev35-50 antibody that results in 50% binding to the rev epitope, based on results with an immunoradiome tric assay, also results in a statistically significant 37% inhibition of HIV-1 replication in human peripheral blood lymphocytes. The catio nized antibodies caused no measurable toxicity to the cells, on the ba sis of [H-3]thymidine incorporation. These studies demonstrate that ca tionization results in enhanced endocytosis of the antibody and enhanc ed inhibition of HIV-1 replication, consistent with intracellular immu nization of the rev protein.