Struggling with low antibody specificity or unreliable neutralization assays in VZV research? Creative Biolabs' VZV gHgL specific Neutra™ antibody products overcome these challenges through advanced conformational epitope mapping and high-throughput validation, enabling precise targeting of viral entry mechanisms to accelerate therapeutic development.
Varicella-zoster virus glycoproteins gHgL (VZV gHgL) form a heterodimeric complex critical for viral entry into host cells. These envelope glycoproteins mediate receptor binding and membrane fusion during infection, making them indispensable for VZV pathogenesis. Expressed during the lytic phase, gHgL is highly conserved across herpesviruses, yet its structural dynamics in VZV are unique, driving species-specific tropism.
The gHgL complex adopts a multi-domain architecture: gH contains transmembrane helices for membrane anchoring, while gL stabilizes its extracellular conformation. Cryo-EM studies reveal that gHgL interacts with host heparan sulfate proteoglycans (HSPGs) for initial attachment. Post-binding, pH-dependent conformational changes expose fusion loops, enabling endosomal entry. Unlike other herpesviruses, VZV gHgL uniquely integrates with the viral tegument protein ORF20, facilitating efficient cell-to-cell spread.
VZV infection activates interferon (IFN) pathways and NF-κB-mediated inflammatory responses. gHgL binding to HSPGs triggers PI3K/Akt signaling, promoting viral internalization. Concurrently, gHgL modulates MHC-I antigen presentation to evade cytotoxic T-cell recognition, ensuring immune evasion and persistent latency in sensory ganglia.
Fig.1 The VZV life cycle.1
VZV causes varicella (chickenpox) during primary infection and herpes zoster (shingles) upon reactivation. In immunocompromised individuals, severe complications include encephalitis and disseminated zoster. The gHgL complex is pivotal for both primary infection and reactivation, driving neurotropism and systemic dissemination.
Fig.2 The potential mechanism of VZV vasculopathy.1
gHgL-specific neutralizing antibodies are vital for assessing vaccine immunogenicity. By quantifying antibody titers in vaccinated cohorts, researchers correlate neutralization capacity with clinical protection, guiding adjuvant selection and dose optimization.
Monoclonal anti-gHgL antibodies reduce viral shedding in zoster patients by >90% in preclinical models. Early administration post-symptom onset lowers neural inflammation and prevents postherpetic neuralgia, offering a targeted alternative to antivirals.
High-affinity anti-gHgL antibodies enable ELISA-based serology kits to distinguish acute infections (IgM/IgA detection) from past exposure (IgG quantification). These tools are critical for rapid diagnosis in outbreaks and monitoring immunosuppressed patients.
Neutralizing antibodies targeting gHgL disrupt viral entry by two mechanisms:
- Blocking Receptor Engagement: Antibodies binding to gHgL's HSPG-interacting domain prevent initial attachment.
- Inhibiting Membrane Fusion: Conformational antibodies lock gHgL in pre-fusion states, halting endosomal fusion.
Creative Biolabs' VZV gHgL-specific antibodies are rigorously validated for specificity (>99% cross-reactivity exclusion) and neutralization potency (EC50 ≤ 2 nM). Applications span therapeutic candidate screening, structural studies, and vaccine efficacy testing.
Creative Biolabs delivers cutting-edge VZV gHgL specific Neutra™ antibody products, engineered to address challenges in virology research and therapeutic development. Our antibodies combine unmatched specificity with functional validation, empowering breakthroughs in vaccine design and precision therapeutics.
Contact our team today to discuss your project needs and explore customized solutions.
Anti-VZV gHgL Neutralizing Antibody (V3S-0522-YC7915) (CAT#: V3S-0522-YC7915)
Target: VZV gHgL
Host Species: Human
Target Species: Varicella-zoster virus (VZV),
Application: Neut,