Recombinant Human Anti-HCV E2 Antibody (HC33.1) (CAT#: PABL-119)

Recombinant Human Antibody (HC33.1) is capable of binding to HCV E2, expressed in HEK 293 cells. Expressed as the combination of a heavy chain (HC) containing VH from anti-HCV E2 mAb and CH1-3 region of human IgG1 and a light chain (LC) encoding VL from anti-HCV E2 mAb and CL of human kappa light chain. Exists as a disulfide linked dimer of the HC and LC hetero-dimer under non-reducing condition. This antibody could neutralize virus bearing the Asn417Ser mutation.


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Figure 2 (A) Epitope alignment. Epitopes of three HMAbs: HC33.1; HC33.4 and HC33.8 are compared with murine MAb AP33. Recombinant E1E2 mutant proteins were expressed in 293T cells and cell lysates were analyzed by ELISA. Individual protein expression was normalized by binding of CBH-17, an anti-HCV E2 HMAb to a linear epitope. Red indicates 0–20%, orange 21–40%, brown 41–60%, white 61–100% and green >100% binding, when the residue was replaced by alanine, relative to binding to wt.

Figure 2 (A) Epitope alignment. Epitopes of three HMAbs: HC33.1; HC33.4 and HC33.8 are compared with murine MAb AP33. Recombinant E1E2 mutant proteins were expressed in 293T cells and cell lysates were analyzed by ELISA. Individual protein expression was normalized by binding of CBH-17, an anti-HCV E2 HMAb to a linear epitope. Red indicates 0–20%, orange 21–40%, brown 41–60%, white 61–100% and green >100% binding, when the residue was replaced by alanine, relative to binding to wt.

Keck, Z. Y., Angus, A. G., Wang, W., Lau, P., Wang, Y., Gatherer, D.,... & Foung, S. K. (2014). Non-random escape pathways from a broadly neutralizing human monoclonal antibody map to a highly conserved region on the hepatitis C virus E2 glycoprotein encompassing amino acids 412–423.PLoS pathogens, 10(8), e1004297.

Figure 3 Dose-dependent neutralization of (B) wt JFH-1 HCVcc, (C) HCVcc variant bearing N417S mutation and (D) bearing N417T mutation were performed by SEAP reporter assay. (B, C, D) Either wt HCVcc or variant HCVcc was incubated with HC33.1 or AP33, at concentrations ranging from 0.1 to 50 µg/ml, prior to infecting the Huh7J-20 cells. Virus infectivity levels were determined by measurement of the SEAP activity released into the medium.

Figure 3 Dose-dependent neutralization of (B) wt JFH-1 HCVcc, (C) HCVcc variant bearing N417S mutation and (D) bearing N417T mutation were performed by SEAP reporter assay. (B, C, D) Either wt HCVcc or variant HCVcc was incubated with HC33.1 or AP33, at concentrations ranging from 0.1 to 50 µg/ml, prior to infecting the Huh7J-20 cells. Virus infectivity levels were determined by measurement of the SEAP activity released into the medium.

Keck, Z. Y., Angus, A. G., Wang, W., Lau, P., Wang, Y., Gatherer, D.,... & Foung, S. K. (2014). Non-random escape pathways from a broadly neutralizing human monoclonal antibody map to a highly conserved region on the hepatitis C virus E2 glycoprotein encompassing amino acids 412–423.PLoS pathogens, 10(8), e1004297.

Figure 4 (A) Dual antibody immunofluorescence staining of Huh7.5 cells infected with JFH1 2a HCVcc during multiple passages in increasing concentration of HC33.1. IFA is shown for P0, P18, P27 and P31. HCV E2 glycoprotein was stained with HC33.1 under which viral escape variants were selected (green, upper set of panels), or with CBH-5, a neutralizing domain B HMAb that does not share the same epitope with HC33.1 on E2 (green, lower set of panels). Total virus-infected cells were stained with anti-NS3 antibody labeled with Alexa-594 (red). The cells were counterstained with Hoechst nuclear stain H33342 (blue). The captured images were superimposed (merge).

Figure 4 (A) Dual antibody immunofluorescence staining of Huh7.5 cells infected with JFH1 2a HCVcc during multiple passages in increasing concentration of HC33.1. IFA is shown for P0, P18, P27 and P31. HCV E2 glycoprotein was stained with HC33.1 under which viral escape variants were selected (green, upper set of panels), or with CBH-5, a neutralizing domain B HMAb that does not share the same epitope with HC33.1 on E2 (green, lower set of panels). Total virus-infected cells were stained with anti-NS3 antibody labeled with Alexa-594 (red). The cells were counterstained with Hoechst nuclear stain H33342 (blue). The captured images were superimposed (merge).

Keck, Z. Y., Angus, A. G., Wang, W., Lau, P., Wang, Y., Gatherer, D.,... & Foung, S. K. (2014). Non-random escape pathways from a broadly neutralizing human monoclonal antibody map to a highly conserved region on the hepatitis C virus E2 glycoprotein encompassing amino acids 412–423.PLoS pathogens, 10(8), e1004297.

Figure 5 (A) HC33.1 dose-dependent neutralization against viral pool in culture supernatants collected from P0, P18, P27 and P34 with their respective dominant variants bearing the following mutations: N417S, N417T/N434D/K610R, N417T/S419N/N434D/K610R and S395/L413I/N417T was performed by FFU-reduction assay.

Figure 5 (A) HC33.1 dose-dependent neutralization against viral pool in culture supernatants collected from P0, P18, P27 and P34 with their respective dominant variants bearing the following mutations: N417S, N417T/N434D/K610R, N417T/S419N/N434D/K610R and S395/L413I/N417T was performed by FFU-reduction assay.

Keck, Z. Y., Angus, A. G., Wang, W., Lau, P., Wang, Y., Gatherer, D.,... & Foung, S. K. (2014). Non-random escape pathways from a broadly neutralizing human monoclonal antibody map to a highly conserved region on the hepatitis C virus E2 glycoprotein encompassing amino acids 412–423.PLoS pathogens, 10(8), e1004297.

Figure 6 Dose-dependent neutralization against recombinant HCVcc variants bearing specific mutations, as identified in each phase of viral escape selection was performed by SEAP reporter assay. The IC50 value against each variant is tabulated in the legend.

Figure 6 Dose-dependent neutralization against recombinant HCVcc variants bearing specific mutations, as identified in each phase of viral escape selection was performed by SEAP reporter assay. The IC50 value against each variant is tabulated in the legend.

Keck, Z. Y., Angus, A. G., Wang, W., Lau, P., Wang, Y., Gatherer, D.,... & Foung, S. K. (2014). Non-random escape pathways from a broadly neutralizing human monoclonal antibody map to a highly conserved region on the hepatitis C virus E2 glycoprotein encompassing amino acids 412–423.PLoS pathogens, 10(8), e1004297.


Specifications

  • Immunogen
  • Hepatitis C virus E2 envelope protein
  • Host Species
  • Human
  • Derivation
  • Human
  • Type
  • IgG
  • Specificity
  • Tested positive against native HCV E2
  • Species Reactivity
  • HCV
  • Clone
  • HC33.1
  • Applications
  • ELISA, Neut, FuncS, IF

Product Property

  • Purity
  • >95% by SDS-PAGE and HPLC analysis
  • Storage
  • Store the antibody (in aliquots) at -20°C. Avoid repeated freezing and thawing of samples.

Applications

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

Target

  • Alternative Names
  • E2; HCV; envelope protein; hepatitis C virus

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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Single-domain Antibody

CAT Product Name Application Type
PNBL-019 Recombinant Anti-HCV E2 VHH Single Domain Antibody (D03) Inhib, FuncS Llama VHH

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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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