Nucleocytoplasmic transport of the Rev protein of human immunodeficiency virus type 1 is dependent on the activation domain of the protein.

The human immunodeficiency virus type 1 (HIV-1) regulatory protein Rev, which is required for the cytoplasmic expression of unspliced and incompletely spliced viral mRNAs, is located predominantly in the nucleolus. In this study, we show that Rev translocates from the nucleolus to the cytoplasm in HeLa and COS cells transfected with Rev under conditions where rRNA synthesis is inhibited (e.g.

CD4-derived peptide and sulfated polysaccharides have similar mechanisms of anti-HIV activity based on electrostatic interactions with positively charged gp120 fragments.

The mechanism of antiviral activity of the CD4-derived peptide 75-99 was compared with that of sulfated polysaccharides. A set of peptides representing all the high positive charge density regions of gp120 and gp41 was used to determine whether electrostatic interactions occur between these negatively charged agents and positively charged HIV envelope fragments. Synthetic peptide AZ2, amino acids 75-99 from V1 CD4, KIEDSDTYIC(Acm)-EVEDQKEEVQLLVFG, and dextran sulfate 500,000 (DS 500) were used as inhibitory agents of antibody binding in ELISA using: (1) anti-peptide rabbit antibodies; (2) sera from HIV infected persons.

Analysis of the fine structure of the antigenic determinants of the transmembrane protein in the HIV coat with chemically modified synthetic peptides.

The amino acids involved in IgG reactivity to four HIV-1 gp41 overlapping synthetic peptides from the sequence 584-624 have been determined by a method based on the chemical modification of trifunctional amino acids, especially the acetylation of the amino groups of the lysine residues at pH 8-9. The reactivities of the sera from HIV-infected individuals and gp41-specific human Mab were studied with the overlapping peptides and their modified forms in indirect and competitive ELISA. Peptides 584-602 and 609-624 (CN-185) reacted with 88% of HIV-positive sera; the highest diagnostic significance (100%) was found with peptides 584-611 (AS-551) and 603-624 (CN-191).