Mouse Anti-HIV-1 Env Recombinant Antibody (clone 8H3) (CAT#: MRO-2820CQ)

Figure 1 Cross clade reactivity of mAbs to a panel of divers HIV-1 envelope proteins.

HIV-1 Env proteins (100 ng/each) from five subtypes (A, B, C, D and F), a circulating recombinant (CRF01_AE), a group M consensus (CON), and an SIVcpzUS1 (SIV) was tested with newly characterized mAbs.

Broadly Reactive Monoclonal Antibodies to Multiple HIV-1 Subtype and SIVcpz Envelope Glycoproteins

Figure 2 HIV-1 Consensus Envelope-Induced Broadly Binding Antibodies.

HIV-1 Consensus Envelope-Induced Broadly Binding Antibodies

Figure 3 18F11 binds HIV-1 Env in a glycan-dependent manner.

HIV-1 Consensus Envelope-Induced Broadly Binding Antibodies

Figure 4 A32 binding is competitively inhibited by C1 antibodies.

C1-specific antibodies 3B3 block biotinylated A32 binding to A244 gp120 monomeric Env, consistent with the binding profile of A32 for C1 Env region.

HIV-1 Consensus Envelope-Induced Broadly Binding Antibodies

Figure 5 Cross-blocking between E2 specific monoclonal antibodies.

EL1SA was carried out using microplates coated with purified E2 and pre-incubated with buffer or buffer containing the E2 MAb, 8C11, 13D8 or 8H3 and then allowed to react with the indicated HRP labeled antibodies as described in Section 2.

Analysis of hepatitis E virus neutralization sites using monoclonal antibodies directed against a virus capsid protein

Figure 6 E2 specific MAb binding curves.

Analysis of hepatitis E virus neutralization sites using monoclonal antibodies directed against a virus capsid protein

Figure 7 Binding of p239 to five cell lines.

p239 binding and penetration. Binding was conducted in the presence of the peptide alone or the peptide plus the p239-specific mAb 8C11 or 8H3, and cell-bound p239 was detected by immunofluorescence and examined under a confocal microscope. Bar, 10 μm.

Putative receptor-binding sites of hepatitis E virus