Recombinant Human Anti-EV71 Antibody (E1) (CAT#: HPAB-0228-FY)

Figure 1 In vivo cross-protection of HBc-E1/2 to EV71 and CA16.

(A) Groups of one-day old BALB/c mice born to female mice immunized with HBc-E1/2, HBc-E1, HBc-E2 or adjuvant with an immunization dose of 100 μg were challenged with pSVA-MP4 or CA16-190. The mortality were monitored and recorded daily for 20 days. The representative results of two independent experiments are shown. (B) Contrast of pathological changes between HBc-E1/2 group and adjuvant group. Mice born to HBc-E1/2 or adjuvant immunized female mice and challenged with pSVA-MP4 or CA16-190 were sacrificed, and the tissues were collected as described in the Materials and Methods. Representative sections analyzed by immunohistochemistry (IHC) or hematoxylin and eosin (HE) staining are shown.

Xu, L. , He, D. , Yang, L. , Li, Z. , Ye, X. , & Yu, H. , et al. (2015). A broadly cross-protective vaccine presenting the neighboring epitopes within the vp1 gh loop and vp2 ef loop of enterovirus 71. Scientific Reports, 5(1), 12973.

Figure 2 Kinetics of anti-epitope antibody responses.

Groups of five mice were immunized with 0.625, 1.25, 10 and 100 μg/dose i.p. at weeks 0, 2 and 4 with HBc-E1/2, HBc-E1, HBc-E2 or HBc(aa1-149) as described in the Materials and Methods. Sera were collected at 0, 2, 4, 6, 8, 10 and 12 for the serological tests and analyzed by ELISA to measure the epitope-specific antibody response, the VP1(aa208-222)-specific antibody response (A,C,E,G) and the VP2(aa141-155)-specific antibody response (B,D,F,H). All serum samples were prepared using 10-fold dilution series, and the first dilution was 100-fold. Each point represents the mean reciprocal log10 endpoint titers and standard error.

Xu, L. , He, D. , Yang, L. , Li, Z. , Ye, X. , & Yu, H. , et al. (2015). A broadly cross-protective vaccine presenting the neighboring epitopes within the vp1 gh loop and vp2 ef loop of enterovirus 71. Scientific Reports, 5(1), 12973.

Figure 3 Analysis of chimeric VLPs.

(A) Schematic presentation of the chimeric HBc protein construct. (B) SDS-PAGE and Western blot analyses of the E. coli-expressed HBc fusion proteins. Lane M, molecular mass marker; Lane 1, HBc-E1/2; lane 2, HBc-E1; lane 3, HBc-E2; lane 4, HBc (aa1-149). (C) Electron microscopy of HBc-E1/2, HBc-E1, HBc-E2 and HBc(aa1-149) VLPs. (D) Molecular modeling of chimeric VLPs and the VP1(aa208-222) and VP1(aa141-155) epitopes located on the surface of HBc VLPs colored by red and green, respectively. These two epitopes are also shown in the mature EV71 virion (PDB ID:3VBS).

Xu, L. , He, D. , Yang, L. , Li, Z. , Ye, X. , & Yu, H. , et al. (2015). A broadly cross-protective vaccine presenting the neighboring epitopes within the vp1 gh loop and vp2 ef loop of enterovirus 71. Scientific Reports, 5(1), 12973.

Figure 4 Analysis of the affinity of anti-VP2(aa141-155) and anti-VP1(aa208-222) against authentic EV71 and CA16 particles.

(A,B) Anti-epitope antibody responses. (C,D) The anti-EV71 (C) and anti-CA16 antibody titers (D) of immune sera from mice immunized with VLPs. (E,F) Immunofluorescence assay of EV71 and CA16 infected RD cells. Immunized mouse sera were diluted 1:100 with PBS and then used to measure epitope-specific antibodies by ELISA with (A) VP1- or (B) VP2-derived epitope peptides as the coating antigen as described in the Materials and Methods. Each symbol represents one mouse.

Xu, L. , He, D. , Yang, L. , Li, Z. , Ye, X. , & Yu, H. , et al. (2015). A broadly cross-protective vaccine presenting the neighboring epitopes within the vp1 gh loop and vp2 ef loop of enterovirus 71. Scientific Reports, 5(1), 12973.