VACV D8 Specific Neutra™ Antibody Products

Are you presently encountering difficulties in advancing potent immunotherapeutics or vaccines targeting poxviruses? Our VACV D8 Specific Neutra™ Antibody Products help you develop highly specific and potent neutralizing antibodies through innovative protein engineering techniques and rigorous validation processes.

Overview of VACV D8

VACV protein D8 is key for viral entry, mediating host cell attachment. Understanding its structure, function, and antibody interactions is vital for developing poxvirus countermeasures. Detailed investigations are imperative.

• Basic Information: VACV D8, an indispensable protein localized on the vaccinia virus surface. It exhibits high conservation across diverse poxviruses. VACV D8 functions as an immunodominant antigen, provoking a robust antibody response within infected hosts. D8 is first synthesized as a precursor, then undergoes subsequent cleavage into two distinct subunits. Mature D8 protein anchored to the membrane facilitates the initial attachment of the virus to host cells, and this attachment phase determines the subsequent course of infection.
• Structure: The D8 protein exhibits a distinct carbonic anhydrase (CAH) fold. Its function is catalyzing carbon dioxide and water conversion. Chondroitin sulfate (CS) is engaged with this structural motif of D8 on host cell surfaces. This interaction is important for viral attachment, facilitating subsequent entry and infection. Crystallographic analyses of D8 complexed with neutralizing antibodies showed the antibody-binding site as comprising discontinuous regions, which collectively form a high-affinity epitope. Consequently, the unique structural adaptation of the CAH fold in D8 allows for specific and crucial interaction with host cells.

Fig. 1 Structure of VACV D8 binding to its ligand chondroitin sulfate E.¹

• Related Signaling Pathways: D8 facilitates VACV attachment to host cells via CS binding, initiating viral entry. While D8 doesn't directly influence intracellular signaling, its role in entry is pivotal for viral replication. Antibodies targeting D8 can inhibit this interaction, neutralizing the virus.

Fig. 2 Interplay between host anti-viral DNA sensing and viral antagonism by VACV. ²

Application of Anti-VACV D8 Antibody

Anti-VACV D8 antibodies have significant potential in both research and clinical applications.

• Vaccine Development: Anti-VACV D8 antibodies serve as critical serological correlates to validate vaccine candidates, quantifying neutralizing antibody titers through standardized assays (e.g., ELISA, PRNT) that directly reflect vaccine-induced immunogenicity. By establishing neutralization thresholds against D8—the viral hemagglutinin mediating cell surface attachment—researchers benchmark protective efficacy, linking antibody avidity to viral entry blockade. These immunoglobulins further act as virological benchmarking standards, calibrating assay specificity to exclude false-positive interference from heterologous orthopoxvirus antigens. This dual utility—efficacy metric and quality control—sharpens preclinical evaluation, ensuring robust data pipelines for next-generation smallpox vaccine development.
• Development of Novel Therapeutics: Anti-VACV D8 antibodies, engineered to neutralize poxvirus infectivity, function by targeting the D8 responsible for CS-mediated host-cell adhesion—precluding virion endocytosis and genomic uncoating. Preclinical in vivo models demonstrate these antibodies reduce viral titers, outperforming traditional antiviral drugs in curbing disseminated infection.

Creative Biolabs provides VACV D8 Specific Neutra™ Antibody Products characterized by high specificity and affinity. These antibodies are tailored to meet the rigorous demands of research in poxvirus biology, vaccine development, and antiviral therapy applications.

REFERENCES

1. Matho, Michael H., et al. "Murine anti-vaccinia virus D8 antibodies target different epitopes and differ in their ability to block D8 binding to CS-E." PLoS pathogens 10.12 (2014): e1004495. Distributed under Open Access license CC BY 4.0, only part A of the original picture. https://doi.org/10.1371/journal.ppat.1004495
2. El-Jesr, Misbah, Muad Teir, and Carlos Maluquer de Motes. "Vaccinia virus activation and antagonism of cytosolic DNA sensing." Frontiers in Immunology 11 (2020): 568412. Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.3389/fimmu.2020.568412