HCV E1/E2 Specific Neutra™ Antibody Products

Are you facing challenges in HCV therapeutic development, such as prolonged antibody validation timelines or insufficient neutralizing efficacy? Creative Biolabs' HCV E1/E2 specific Neutra™ antibody products leverage advanced recombinant engineering and structural epitope mapping to deliver high-specificity antibodies that enable rapid target validation, therapeutic screening, and diagnostic assay development.

Introduction to HCV E1/E2

The Hepatitis C virus E1/E2 complex, a heterodimeric envelope glycoprotein, is central to viral entry and immune evasion. E1 and E2 are post-translationally modified, highly glycosylated proteins that mediate host cell attachment via interactions with receptors such as CD81, SR-B1, and Claudin-1. As the primary target for neutralizing antibodies, the E1/E2 complex's structural plasticity and hypervariable regions pose significant challenges in antibody development, necessitating precise targeting of conserved epitopes.

• Structural Insights

E1 (192-340 residues) and E2 (384-661 residues) form a metastable heterodimer stabilized by non-covalent interactions. The E2 ectodomain contains a conserved receptor-binding domain (RBD) and a flexible hypervariable region 1 (HVR1), while E1 contributes to membrane fusion through its N-terminal α-helix. Cryo-EM studies reveal that E1/E2 adopts multiple conformational states during viral entry, with neutralizing antibodies preferentially targeting the RBD and adjacent conserved epitopes.

Fig.1 Expression and processing of membrane-bound E1E2 (mbE1E2) complex.¹

• Signaling and Pathogenicity

HCV exploits host MAPK and interferon signaling pathways to evade immune detection. E2's engagement with CD81 downregulates antiviral interferon responses, facilitating persistent infection. Chronic HCV infection progresses to cirrhosis, hepatocellular carcinoma, and liver failure, underscoring the urgent need for therapeutics targeting E1/E2-mediated entry.

Applications of HCV E1/E2 Neutralizing Antibodies

• Therapeutic Candidate Development

Neutralizing mAbs are pivotal in passive immunotherapy, reducing viral load in acute infections. Antibodies targeting conserved E2 epitopes show synergistic effects with direct-acting antivirals (DAAs), enhancing sustained virologic response rates in clinical trials.

• Vaccine Design and Evaluation

E1/E2-based vaccine candidates rely on neutralizing antibodies to elicit durable immunity. Antibodies validate antigenic integrity in vaccine formulations and assess humoral responses in preclinical models, bridging structural insights to immunogenicity.

• Diagnostic Assay Optimization

High-specificity antibodies enable early HCV detection in serological assays. They differentiate active infections from resolved cases by detecting E1/E2 immune complexes, improving diagnostic accuracy in high-risk populations.

• Antiviral Mechanism Studies

Antibodies dissect E1/E2-receptor interactions and fusion mechanisms. Competitive binding assays identify epitopes critical for neutralization, guiding rational antibody engineering and combination therapy strategies.

Antibodies Against HCV E1/E2

Neutralizing antibodies targeting HCV E1/E2 block viral attachment, receptor engagement, or membrane fusion. High-affinity monoclonal antibodies (mAbs) against the E2 RBD or E1/E2 interdomain interfaces demonstrate cross-genotypic neutralization in vitro and in vivo. Creative Biolabs' antibodies are engineered using mammalian cell-based systems to preserve conformational epitopes, ensuring superior specificity for functional studies and therapeutic applications.

Creative Biolabs' HCV E1/E2 specific Neutra™ antibody products empower researchers to overcome bottlenecks in therapeutic discovery and diagnostic innovation. With rigorously validated specificity and cross-genotypic efficacy, our antibodies are essential tools for advancing HCV research.

Contact our scientific team to explore customized solutions for your project.

REFERENCE

1. Toth, Eric A., et al. "Structural and biophysical characterization of the HCV E1E2 heterodimer for vaccine development." Viruses 13.6 (2021): 1027. Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.3390/v13061027