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1.
Figure 3

Figure 3. Evaluation of P1 and P2-induced neutralizing activity in an Env-based pseudovirus assay.. From: Anti-HIV-1 Response Elicited in Rabbits by Anti-Idiotype Monoclonal Antibodies Mimicking the CD4-Binding Site.

Data are reported as reciprocal of serum dilutions giving 80% of pseudovirus neutralization (ID80). Neutralization data on Murine Leukemia Virus (MuLV) are also reported as control. For sample shortage due to technical problems it was not possible to perform the assay with sera from rabbit # 8 (P1 group), and for rabbits # 15 and # 17 (P2 group) on MN and HXB2 pseudoviruses, respectively.

Roberto Burioni, et al. PLoS ONE. 2008;3(10):e3423.
2.
Figure 2

Figure 2. Evaluation of P1 and P2-induced antibody response in rabbits and of its neutralizing activity in an Env-based pseudovirus assay.. From: Anti-HIV-1 Response Elicited in Rabbits by Anti-Idiotype Monoclonal Antibodies Mimicking the CD4-Binding Site.

ELISA titers of preimmune (black) and immune (red) rabbits' sera on gp120 IIIB (continuous line) and BSA (dotted line) after three immunizations with the reported antigens. Data regarding the gp120 (positive control) and the J1 (negative control) groups are not reported, but for all animals the titers were >1∶12800 and <1∶25, respectively. Moreover, among the animals immunized with the mouse mAbs, no difference was evidenced in terms of response elicited against the specific molecule used for the immunizations (data not shown).

Roberto Burioni, et al. PLoS ONE. 2008;3(10):e3423.
3.
Figure 1

Figure 1. Characterization of P1 and P2 binding features.. From: Anti-HIV-1 Response Elicited in Rabbits by Anti-Idiotype Monoclonal Antibodies Mimicking the CD4-Binding Site.

(a) Recognition of P1 and P2 putative AI molecules by anti-gp120 mAbs. ELISA wells coated with P1, P2, gp120 IIIB (YU2) as positive control, or BSA (negative control) were reacted with: I) four anti-CD4bs mAbs: b12 (1.4 µg/ml), F105 (1.5 µg/ml), 654-30D (1 µg/ml) and GP68 (1 µg/ml); II) two anti-V3 mAbs: F425 B4e8 (1.5 µg/ml) and 447-52D (1 µg/ml); III) one anti-C5 mAb: 670-30D (0.4 µg/ml) and IV) one anti-CD4 induced epitope mAb 17b (1 µg/ml). All monoclonals were obtained through the NIH AIDS Research and Reference Reagent Program, Division of AIDS, NIAID, NIH. Interestingly, P1 and P2 were specifically recognized only by b12, the most potent mAb used in this study in terms of neutralizing activity on primary isolates. The AI molecules were also tested with different preparations of standard IgG and with all serum fractions discarded during the purification process of anti-CD4bs IgG, giving in all cases a negative result (data not shown). (b) Titration of b12 on P1, P2, gp120 and BSA. (c) Competition ELISA. The ability of P1 and P2 to inhibit the binding of b12 to immobilized gp120 was tested in a competition ELISA. 96-well flat bottom plate wells were coated overnight at 4°C with HIV-1 YU2 gp120 (100 ng/well) and then blocked with 1% BSA-PBS. b12 (1 µg/ml) and serial dilutions (from 10−5 M to 10−12 M) of P1, P2 and J1 control mAb were added to the wells. b12 residual binding was detected with enzyme-linked goat anti-human IgG.

Roberto Burioni, et al. PLoS ONE. 2008;3(10):e3423.

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