HIV gp120 Specific Neutra™ Antibody Products
Product listStruggling with challenges in HIV therapeutic antibody development or inconsistent neutralization data? Creative Biolabs' HIV gp120 specific Neutra™ antibodies integrate advanced structural biology and precision engineering to deliver high-affinity solutions, accelerating antiviral drug discovery and vaccine development.
Introduction to HIV gp120
HIV gp120, a glycoprotein subunit of the viral envelope trimer (gp120-gp41 complex), is critical for host cell entry. It mediates viral attachment by binding to CD4 receptors and chemokine co-receptors (CCR5/CXCR4) on immune cells. As the primary target for neutralizing antibodies, gp120's hypervariable regions (V1-V5) drive immune evasion, while conserved epitopes enable cross-clade neutralization.
- Structural Dynamics
The gp120 core consists of inner and outer domains stabilized by disulfide bonds. The V3 loop, a key neutralizing determinant, undergoes conformational shifts during receptor binding, exposing hidden epitopes. Cryo-EM studies reveal that gp120 adopts a "closed" conformation in prefusion trimers, shielding vulnerable sites. Targeted mutations, such as those stabilizing the CD4-bound state, enhance antigenicity for antibody development.
- Receptor Engagement and Signaling
Upon CD4 binding, gp120 triggers co-receptor interaction, activating host cell signaling cascades. This process recruits actin-modifying proteins to facilitate membrane fusion and viral entry. Notably, gp120 binding inhibits interferon (IFN) signaling in dendritic cells, impairing antiviral immunity—a mechanism exploited by HIV for immune evasion.
Fig.1 Mechanism of HIV-gp120/CD4 entry.1
- Pathological Implications
HIV gp120 drives viral pathogenicity by enabling persistent infection of CD4+ T cells and macrophages, leading to progressive immune depletion. Chronic infection results in AIDS, characterized by opportunistic infections and malignancies. Despite antiretroviral therapy, latent reservoirs and gp120 variability limit cure strategies, emphasizing the need for neutralizing antibodies.
Translational Applications of HIV gp120 Neutralizing Antibodies
- Therapeutic Neutralization
Monoclonal antibodies targeting gp120 block viral entry and reduce viral load in clinical trials. Passive immunization with bnAbs (broadly neutralizing antibodies) shows promise in pre-exposure prophylaxis (PrEP) and post-exposure treatment, particularly for high-risk populations.
- Vaccine Development
Engineered gp120 trimers, stabilized in prefusion states, serve as immunogens to elicit bnAbs. These antibodies are instrumental in evaluating antigen integrity and immunogenicity during vaccine formulation.
- Diagnostic Advancements
High-affinity anti-gp120 antibodies underpin sensitive assays for viral load quantification and reservoir detection. These tools aid in monitoring treatment efficacy and disease progression.
- Host-Pathogen Research
Antibodies facilitate studies on gp120-receptor interactions, immune evasion mechanisms, and latency reversal strategies. This supports the development of novel entry inhibitors and immune therapies.
Antibodies Targeting HIV gp120
Creative Biolabs offers HIV gp120 specific Neutra™ antibodies with unmatched specificity for advancing therapeutics, diagnostics, and virology research. Neutralizing antibodies against gp120 block receptor binding or fusion by recognizing:
1. CD4-binding site (CD4bs): Mimic CD4 interactions, preventing viral attachment.
2. V3 loop: Target the glycoprotein's mutable yet functionally conserved region, critical for co-receptor engagement.
3. Glycan-dependent epitopes: Bind quaternary epitopes stabilized by N-linked glycans.
Our gp120-specific antibodies are engineered for high specificity to conformational epitopes, validated in neutralization assays and structural studies. These reagents enable epitope mapping, vaccine candidate screening, and therapeutic potency evaluation.
Contact our team to discuss custom solutions for your HIV research needs.
REFERENCE
- Zuru, Danlami Umar. "Theoretical model for the design and preparation of a CNT–ursonic acid drug matrix as HIV-gp120 entry inhibitor." Scientific African 6 (2019): e00177. Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.1016/j.sciaf.2019.e00177
