RABV Specific Neutra™ Antibody Products
Product listCreative Biolabs provides a suite of top-tier antibodies and related tools crafted to support your rabies virus research from initiation to completion. Our products and services deliver the specificity and sensitivity you require for precise and dependable outcomes. We recognize that effective rabies virus research relies on the capacity to accurately and reliably identify and analyze viral antigens, a core principle in our antibody design. Whether your work involves basic investigation, the creation of new diagnostic methods, or the exploration of innovative treatment approaches, our tools lay the groundwork for strong and significant discoveries. Our dedication goes beyond simply supplying reagents; we strive to be a collaborative ally in your scientific pursuits, offering the knowledge and assistance necessary to maximize the impact of your work.
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Introduction of Rabies Virus
Rabies encephalitis, caused by the Lyssavirus genus member rabies virus (RABV), presents a near-absolute case-fatality rate, claiming approximately 59,000 annual fatalities—primarily pediatric (<15 years) in Asia and Africa’s resource-constrained regions. This neuroinvasive Mononegavirales pathogen exhibits strict axonal tropism, exploiting mammalian nicotinic acetylcholine receptors (nAChRs) for centripetal spread to the CNS. While canine-mediated inoculation via lacerations remains the dominant transmission route, sylvatic reservoirs (Chiroptera, Vulpes vulpes) sustain enzootic cycles in high-income nations, including the United States and Russian Federation.
Prophylaxis hinges on pre-exposure immunization or rigorous post-exposure protocols stratified by WHO exposure categories. Category III exposures—defined as transdermal breaches or mucosal contamination by infectious saliva—necessitate immediate wound irrigation followed by post-exposure prophylaxis (PEP): passive immunization with rabies immunoglobulin (RIG) and active vaccination to induce neutralizing anti-glycoprotein IgG titers.
Fig. 1 Rabies Virus.Distributed under CC BY-SA 4.0, from Wiki, without modification
The rabies pathogen, an enveloped (−)ssRNA virus (60×180 nm), comprises a ribonucleoprotein core encapsidating genomic RNA, surrounded by a host-derived lipid bilayer studded with trimeric glycoprotein (G) protrusions. Viral populations diverge into two principal categories: attenuated laboratory strains (passage-adapted) and enzootic wildlife variants maintained in reservoir hosts. Immunological and genomic profiling—leveraging neutralizing monoclonal antibody panels alongside nucleocapsid gene phylogenetics—enables precise discrimination of geographically distinct lineages. This integrated approach proves critical for exposure source attribution in cases lacking documented animal contact, circumventing reliance on traditional epidemiological markers.
Antibodies against RABV
Neutralizing monoclonal antibodies (nAbs) serve as critical biologics in rabies post-exposure prophylaxis (PEP), engineered through two primary strategies: isolation of antigen-specific B lymphocytes from vaccinated donors’ peripheral blood mononuclear cells (PBMCs), or panning of naïve/synthetic phage-displayed combinatorial libraries. These immunotherapeutics exclusively target the rabies glycoprotein (G), engaging distinct subdomains through varied inhibitory modalities. Current models propose four synergistic modes of neutralization: (1) competitive inhibition of viral attachment to host receptors; (2) steric interference with endosomal membrane fusion; (3) suppression of progeny virion egress via cross-linking surface G proteins; and (4) Fc-mediated effector functions including complement-dependent cytolysis (CDC) and antibody-dependent cellular phagocytosis (ADCP).
Fig. 2 Structure of RABV.1
Receptor blockade predominates as the principal mechanism, particularly at the nicotinic acetylcholine receptor (nAChR) interface—the prototypical rabies entry portal. Structural analyses localize the nAChR-binding epitope to G protein residues 173–204 (antigenic site II), explaining why site II-directed nAbs (e.g., RAB1) potently occlude neurotropic invasion.
Beyond receptor antagonism, nAbs disrupt pH-triggered fusogenic rearrangements of the G trimer. Under acidic endosomal conditions, the glycoprotein undergoes a metastable transition from pre-fusion (compact) to post-fusion (elongated) conformations—a process abrogated by nAbs binding quaternary epitopes at domain interfaces. Such steric hindrance prevents the structural gymnastics essential for viral-host membrane coalescence.
Why Choose Us?
Creative Biolabs is your trusted partner for rabies virus antibody solutions. We offer several key advantages:
- Unparalleled Specificity and Sensitivity: Our antibodies are developed and rigorously validated to ensure they meet the highest standards of specificity and sensitivity, minimizing the risk of false positives and false negatives.
- Customizable Solutions: We understand that every research project is unique. We offer flexible and customizable solutions tailored to your specific needs, including custom antibody development, labeling, and conjugation.
- Expert Scientific Support: Our team of experienced scientists provides expert guidance and support throughout your project, from initial consultation to final delivery.
- Stringent Quality Control: We adhere to strict quality control procedures at every stage of antibody development and production to ensure the highest quality and consistency.
For more information about Creative Biolabs' RABV antibodies and services, please contact us.
REFERENCE
- Kiflu, Abraha Bahlbi. "The Immune Escape Strategy of Rabies Virus and Its Pathogenicity Mechanisms." Viruses 16.11 (2024): 1774. Distributed under Open Access license CC BY 4.0, without modification.
