EBOV Specific Neutra™ Antibody Products

Are prolonged therapeutic development timelines or challenges in neutralizing highly mutable viruses hindering your Ebola research? Creative Biolabs' EBOV-specific Neutra™ antibody products leverage advanced recombinant DNA technology and high-throughput epitope mapping to accelerate the development of therapeutics with cross-clade efficacy.

Introduction to EBOV

The Ebola virus (EBOV), a member of the Filoviridae family, is an enveloped, negative-sense RNA virus known for producing severe hemorrhagic fever with fatality rates of up to 90%. Its genome encodes seven structural proteins, including the glycoprotein (GP), which mediates host cell entry and serves as the primary target for neutralizing antibodies.

• Structure

EBOV's surface GP trimer facilitates viral attachment by binding to host receptors like Niemann-Pick C1 (NPC1). The GP undergoes proteolytic cleavage into GP1 (receptor-binding subunit) and GP2 (membrane fusion subunit), with critical epitopes in the GP base region conferring broad neutralization potential. Cryo-EM studies reveal that neutralizing antibodies often target the receptor-binding domain (RBD) or membrane-proximal regions, sterically hindering viral fusion.

• Related Signaling Pathways

EBOV infection disrupts innate immune signaling, particularly type I interferon (IFN) production, by viral proteins VP35 and VP24. These proteins inhibit IFN-α/β synthesis and block nuclear import of transcription factors like STAT1, enabling immune evasion. Neutralizing antibodies counterbalance this by enhancing opsonization and antibody-dependent cellular cytotoxicity (ADCC), restoring immune recognition.

Fig.1 The activation of innate immune responses is interfered with by EBOV.¹

• Associated Diseases

EBOV causes Ebola virus disease (EVD), characterized by fever, hemorrhaging, and multi-organ failure. Outbreaks, such as the 2014–2016 West African epidemic, highlight its public health threat due to human-to-human transmission via bodily fluids and high mutation rates fostering antigenic drift.

Applications of EBOV Neutralizing Antibodies

• Therapeutic Development

Neutralizing antibodies are pivotal in post-exposure prophylaxis and acute treatment. Clinical trials demonstrate that cocktails like REGN-EB3 reduce mortality by 66% when administered early. These antibodies block viral entry via competitive inhibition of GP-NPC1 interactions, minimizing viral load and systemic dissemination.

• Diagnostic Tool Development

High-affinity antibodies enable rapid antigen detection in blood or saliva, critical for outbreak containment. Lateral flow assays incorporating GP-specific antibodies achieve 99% specificity, facilitating point-of-care testing in resource-limited settings.

• Vaccine Efficacy Evaluation

Quantifying neutralizing antibody titers in vaccinated individuals correlates with immune protection. Surrogate neutralization assays using vesicular stomatitis virus (VSV)-EBOV pseudotypes provide a BSL-2-compliant method to assess vaccine-induced immunity.

Our Anti-EBOV Antibodies

Monoclonal antibodies (mAbs) target the GP trimer, blocking receptor engagement or fusion-loop accessibility. For research, neutralizing antibodies enable:

- Quantification of viral load via ELISA or flow cytometry.

- Structural analysis of GP-antibody complexes to refine epitope targeting.

- Preclinical validation of vaccine candidates by correlating antibody titers with protection.

Our antibodies are more than 90% effective at neutralizing Zaire and Sudan ebolavirus strains, validated in pseudovirus and live-virus assays.

Creative Biolabs provides verified EBOV-specific Neutra™ antibody products designed to tackle virological and immunological challenges with Ebola research. Our antibodies are optimized for neutralization assays, structural studies, and therapeutic development.

Contact our scientific team today to discuss customized solutions for your EBOV projects.

REFERENCE

1. He, Felix B., et al. "Innate Immune System." Emerging challenges in filovirus infections (2020): 51. Distributed under Open Access license CC BY 3.0, without modification. http://dx.doi.org/10.5772/intechopen.86749