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. 2014 Feb 3;111(8):3152–3157. doi: 10.1073/pnas.1314718111

Fig. 3.

Fig. 3.

Competition of a tyrosine-sulfated V2 mimetic peptide with mAb 412d binding to gp120. (A) Effect of a tyrosine-sulfated V2-loop mimetic peptide (pV2α-Tys; amino acids 168–185) on mAb 412d binding to gp120 as assessed by surface plasmon resonance. A tyrosine-sulfated peptide derived from the CCR5 N terminus (pCCR5-Tys; amino acids 1–22) and unsulfated peptides from V2 (pV2α) and CCR5 (pCCR5) were tested in parallel as controls. MAb 412d was immobilized on the sensor surface and tested for binding to gp120 (BaL) pretreated with two-domain sCD4 in the presence or absence of the peptides used at 166 μM. A control antibody (F105; no sCD4 pretreatment) was tested in parallel as a control. The data are from a representative experiment of three that were performed with similar results. (B) Effect of tyrosine-sulfated and unsulfated V2-loop and CCR5 N terminus mimetic peptides on HIV-1 virion capture by mAb 412d. Infectious viral stocks from HIV-1 BaL were pretreated with sCD4 (5 μg/mL) in the presence or absence of the indicated peptides (each at 100 μM) and then were mixed with immunomagnetic beads prearmed with mAb 412d. A control antibody (2G12; no sCD4 pretreatment) was tested in parallel as a further specificity control. The data presented are mean values (± SD) from three independent experiments. Asterisks denote significant differences from the virion capture in the peptide-untreated control (P < 0.01 by unpaired Student t test).