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. 2017 Nov 27;7:16335. doi: 10.1038/s41598-017-16451-w

Figure 10.

Figure 10

Antiviral activity of αRep4E3 and αRep9A8. (a), PR-mediated maturation cleavage of Pr55Gag. Control cells (unmodified SupT1 and SupT1/αRep9C2-GFP), and αRep-expressing cells (SupT1/αRep4E3-GFP and SupT1/αRep9A8-GFP) were infected with HIV-1 at the same MOI, and extracellular media collected. After normalization to the CAp24 level (80 µg per sample), the degree of proteolytic cleavage of Pr55Gag at the MA-CA junction by the viral protease (PR) was evaluated using an ELISA-based maturation assay. The bar graph represents the percentage of cleaved Pr55Gag (mean ± SD; n = 3), estimated from the degree of accessibility and reactivity of a Gag-embedded MA epitope towards its specific monoclonal antibody, in competition with a free synthetic peptide reproducing its sequence (refer to Materials & Methods). (b), Viral genome packaging. Bar graph representing the concentrations of HIV-1 genomes in culture media after normalization to CAp24 levels (genome copy number per 25 µg CAp24; mean ± SD; n = 3), and the fold changes in culture media of SupT1/αRep4E3-GFP and SupT1/αRep9A8-GFP cells, compared to control cell lines SupT1 and SupT1/αRep9C2-GFP. (**), P < 0.01; (*), P < 0.05; ns, not significant.