Recombinant Mouse Anti-HCV E2 Antibody (MAb24) (CAT#: PABC-475)

Figure 1 Direct binding of MAbs to E2661 with single and multiple variable region deletions.

Data from two independent analyses of MAb24 reactivity are shown for reproducibility.

ALHAMMAD, Yousef, et al. Monoclonal antibodies directed toward the hepatitis C virus glycoprotein E2 detect antigenic differences modulated by the N-terminal hypervariable region 1 (HVR1), HVR2, and intergenotypic variable region. Journal of virology, 2015, 89.24: 12245-12261.

Figure 2 Ability of MAbs to bind their epitopes on the surface of VLPs.

Ability of MAbs to bind VLPs in a direct binding ELISA.

ALHAMMAD, Yousef, et al. Monoclonal antibodies directed toward the hepatitis C virus glycoprotein E2 detect antigenic differences modulated by the N-terminal hypervariable region 1 (HVR1), HVR2, and intergenotypic variable region. Journal of virology, 2015, 89.24: 12245-12261.

Figure 3 Ability of MAb24 to mediate neutralization of different HCV genotypes.

IC50s and IC90s (micrograms per milliliter) were derived from neutralization assays performed with HCVpp (genotype 1a) and HCVcc (genotypes 2a and 4a to 7a). X indicates that no neutralization was observed at the highest concentration of antibody tested. Data shown are the means standard errors of the means of data from at least three independent experiments. Genotype 3a neutralization was performed by incubating MAb24 with HCVcc and applying this mixture to Huh7.5 cells plated ontocoverslips. Foci were visualized 3 days later after staining with anti-NS5A an-tibody and Alexa 488-labeled anti-mouse antibody. The mean percent reductions in foci on 2 coverslips relative to the no-antibody control and standard deviations are shown. Results are representative of data from two independent experiments.

ALHAMMAD, Yousef, et al. Monoclonal antibodies directed toward the hepatitis C virus glycoprotein E2 detect antigenic differences modulated by the N-terminal hypervariable region 1 (HVR1), HVR2, and intergenotypic variable region. Journal of virology, 2015, 89.24: 12245-12261.

Figure 4 Expression of E2 RBD glycoproteins.

The expression of E2 RBD glycoproteins of patient B derived from concentrated tissue culture fluid of transfected cells immunoprecipitated with anti E2 MAb24, separated using SDS-PAGE under reducing conditions and detected by Western blotting using anti His antibody. Empty = tissue culture fluid of mock transfected cells with pcDNA4c empty vector.

ALHAMMAD, Yousef MO, et al. Longitudinal sequence and functional evolution within glycoprotein E2 in hepatitis C virus genotype 3a infection. PLoS One, 2015, 10.5.

Figure 5 Binding of neutralizing MAb24 to E2 RBD glycoproteins.

E2 RBD glycoproteins were normalized and applied to the ELISA plates coated with GNA-Lectin. Bound E2 RBD glycoproteins from patient B were detected with serially titrated neutralizing anti E2 MAb24 and secondary anti-mouse HRP antibodies.

ALHAMMAD, Yousef MO, et al. Longitudinal sequence and functional evolution within glycoprotein E2 in hepatitis C virus genotype 3a infection. PLoS One, 2015, 10.5.