Human Anti-HIV-1 Env V2 region Recombinant Antibody (clone CH58) (CAT#: PABL-157)

Recombinant Human Antibody (CH58) is capable of binding to HIV-1 env V2 region, expressed in HEK 293 cells. Expressed as the combination of a heavy chain (HC) containing VH from anti-HIV-1 env V2 region mAb and CH1-3 region of human IgG1 and a light chain (LC) encoding VL from anti-HIV-1 env V2 region mAb and CL of human light chain. Exists as a disulfide linked dimer of the HC and LC hetero-dimer under non-reducing condition. This antibody could neutralize laboratory-adapted HIV-1, and mediate killing of field-isolate HIV-1-infected CD4(+) T cells.


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Figure 1 ELISA showing binding to the autologous transmitted/founder CAP228 V1V2 scaffolded protein by wild-type CAP228-16H (green), and the ED-motif mutant (red), when compared to antibodies that naturally contain the ED motif: CAP228-3D (purple), CH58 (blue), and CH59 (gray). Absorbance readings are plotted on the y axis versus mAb concentration on the x axis.

Figure 1 ELISA showing binding to the autologous transmitted/founder CAP228 V1V2 scaffolded protein by wild-type CAP228-16H (green), and the ED-motif mutant (red), when compared to antibodies that naturally contain the ED motif: CAP228-3D (purple), CH58 (blue), and CH59 (gray). Absorbance readings are plotted on the y axis versus mAb concentration on the x axis.

van Eeden, C., Wibmer, C. K., Scheepers, C., Richardson, S. I., Nonyane, M., Lambson, B.,... & Bhiman, J. N. (2018). V2-Directed Vaccine-like Antibodies from HIV-1 Infection Identify an Additional K169-Binding Light Chain Motif with Broad ADCC Activity. Cell reports, 25(11), 3123-3135.

Figure 2 Buried surface area for V2 peptides residues 165–182 (x axis) from the CAP228-16H (purple) or CH58 (green) cocrystal structures, plotted as a percentage of the total accessible surface area (y axis). Significant differences between the two structures are boxed in yellow, and hydrogen bonds (H) or salt bridges (S) are labeled. The potential interaction between CAP228-16H and a sulfated tyrosine at position Y177 is indicated with the asterisk.

Figure 2 Buried surface area for V2 peptides residues 165–182 (x axis) from the CAP228-16H (purple) or CH58 (green) cocrystal structures, plotted as a percentage of the total accessible surface area (y axis). Significant differences between the two structures are boxed in yellow, and hydrogen bonds (H) or salt bridges (S) are labeled. The potential interaction between CAP228-16H and a sulfated tyrosine at position Y177 is indicated with the asterisk.

van Eeden, C., Wibmer, C. K., Scheepers, C., Richardson, S. I., Nonyane, M., Lambson, B.,... & Bhiman, J. N. (2018). V2-Directed Vaccine-like Antibodies from HIV-1 Infection Identify an Additional K169-Binding Light Chain Motif with Broad ADCC Activity. Cell reports, 25(11), 3123-3135.

Figure 3 Synergy of MAb binding to monomeric gp120 by SPR.

Figure 3 Synergy of MAb binding to monomeric gp120 by SPR.

(A) Schematic of the SPR assay utilized to test the presence of synergy between the V2 and C1 MAbs for binding to the recombinant AE.244Δ11 gp120 according to the procedure reported in Materials and Methods. (B) SPR of binding of the CH58 MAb in combination with negative-control MAb Palivizumab and the C1 MAbs A32, 16H3, CH57, CH54, and CH90. The y axis represents the response unit values, and the x axis represents the time in milliseconds. (C) Fold increase of the V2 MAb CH58 binding to the recombinant AE.A244Δ11 gp120. The data are reported as percentage of increase compared to the binding of the CH58 MAb to gp120 incubated with Palivizumab used as negative control.

Pollara, J., Bonsignori, M., Moody, M. A., Liu, P., Alam, S. M., Hwang, K. K.,... & Whitesides, J. F. (2014). HIV-1 vaccine-induced C1 and V2 Env-specific antibodies synergize for increased antiviral activities. Journal of virology, JVI-00156.

Figure 4 Synergy of MAb for binding to the infected CD4 T cells.

Figure 4 Synergy of MAb for binding to the infected CD4 T cells.

Primary CD4+ T cells were activated and infected with HIV-1 AE.92TH023 (A to C) and AE.CM235 (D and E) for 72 h. Cells were stained with viability dye and anti-p24 Ab to identify viable (live) infected (p24+) cells using the gating strategy shown by the dot plot in panel A. The CH58 MAb was conjugated with Alexa Fluor 488 fluoropohore. The other MAbs and MAb Fab fragments (Palivizumab [Neg], A32, CH54, CH57, and CH90) were used as nonconjugated reagents. The histogram in panel A is representative of the CH58 Alexa Fluor-488 staining of infected cells (p24+) observed with individual and combined MAbs. (B to E) The infected CD4+ T cells were stained with CH58 Alexa Fluor 488 in combination with the MAbs or Fab fragments indicated on the x axes at 10 μg/ml each. The y axes represent the percentage of increase of stained cells (B and D) and mean fluorescent intensity (MFI) (C and E) for each combination of MAb or Fab fragment relative to the staining of cells observed when the CH58 MAb was used alone.

Pollara, J., Bonsignori, M., Moody, M. A., Liu, P., Alam, S. M., Hwang, K. K.,... & Whitesides, J. F. (2014). HIV-1 vaccine-induced C1 and V2 Env-specific antibodies synergize for increased antiviral activities. Journal of virology, JVI-00156.

Figure 5 ADCC synergy with combinations of V2 and C1 MAbs.

Figure 5 ADCC synergy with combinations of V2 and C1 MAbs.

(A to E) ADCC synergy with equimolar combinations of V2 and C1 MAbs. Shown is the percentage of specific killing observed by V2 MAbs CH58 (A), CH59 (B), HG107 (C), and HG120 (D) alone and in combination with negative-control Palivizumab or C1 MAbs CH54, CH57, and CH90 at a 1:1 ratio over 5-fold serial dilutions in the luciferase ADCC assay with CM235-infected targets. (E) ADCC synergy with nonequimolar combinations of V2 and C1 MAbs. The percentage of specific killing was detected by incubating individual MAbs and the combinations indicated with HIV-1 AE.CM235-infected CEM.NKRCCR5 target cells for 3 h in the luciferase ADCC assay. The expected ADCC activities for an additive effect are represented by white bars. (F) Synergy of CH58 anti-V2 IgG and CH90 anti-C1 F(ab′)2 for ADCC. The graph represents the percentage of specific killing observed by V2 MAb CH58 and CH90 C1 F(ab′)2 alone and in combination at a 1:1 ratio over 5-fold serial dilutions in the luciferase ADCC assay with CM235-infected targets.

Pollara, J., Bonsignori, M., Moody, M. A., Liu, P., Alam, S. M., Hwang, K. K.,... & Whitesides, J. F. (2014). HIV-1 vaccine-induced C1 and V2 Env-specific antibodies synergize for increased antiviral activities. Journal of virology, JVI-00156.

Figure 6 V2 MAbs synergize with C1 MAb for enhanced selective capture of infectious HIV-1 AE.92TH023 virions.

Figure 6 V2 MAbs synergize with C1 MAb for enhanced selective capture of infectious HIV-1 AE.92TH023 virions.

IVCI (i.e., the fold change of the ratios of infectious HIV-1 AE.92TH023 virions to total virion particles) was used to quantify the selective capture of infectious versus noninfectious virions. (A) IVCI values of V2 MAbs CH58 and C59 and the positive-control gp41 MAb 7B2 when tested alone (black squares) or in combination with the C1 MAb A32 (red circles). (B) Fold increase of IVCI values observed in the presence of C1 MAb A32.

Pollara, J., Bonsignori, M., Moody, M. A., Liu, P., Alam, S. M., Hwang, K. K.,... & Whitesides, J. F. (2014). HIV-1 vaccine-induced C1 and V2 Env-specific antibodies synergize for increased antiviral activities. Journal of virology, JVI-00156.


Specifications

  • Host Species
  • Human
  • Type
  • Human IgG
  • Species Reactivity
  • HIV-1
  • Clone
  • CH58
  • Applications
  • Neut, FuncS

Product Property

  • Purity
  • >95% as determined by SDS-PAGE
  • Concentration
  • Please refer to the vial label for the specific concentration.
  • Buffer
  • PBS
  • Preservative
  • No preservatives
  • Storage
  • Centrifuge briefly prior to opening vial. Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freeze/thaw cycles.

Applications

  • Application Notes
  • The antibody was validated for ELISA, FC and ADCC. For details, refer to published data.

Target

  • Alternative Names
  • ENV; gp160; envelope glycoprotein; Envelope surface glycoprotein gp160; precursor; hypothetical protein; Envelope surface glycoprotein gp120; Envelope transmembrane domain

Product Notes

This is a product of Creative Biolabs' Hi-Affi™ recombinant antibody portfolio, which has several benefits including:

• Increased sensitivity
• Confirmed specificity
• High repeatability
• Excellent batch-to-batch consistency
• Sustainable supply
• Animal-free production

See more details about Hi-Affi™ recombinant antibody benefits.

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scFv Fragment Antibody

CAT Product Name Application Type
PSBL-157 Human Anti-HIV-1 Env V2 region Recombinant Antibody (clone CH58); scFv Fragment Neut, FuncS Human scFv

Fab Fragment Antibody

CAT Product Name Application Type
PFBL-157 Human Anti-HIV-1 Env V2 region Recombinant Antibody (clone CH58); Fab Fragment Neut, FuncS Human Fab

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For research use only. Not intended for any clinical use. No products from Creative Biolabs may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative Biolabs.

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