CPV Capsid Protein Specific Neutra™ Antibody Products

Are you grappling with prolonged antibody development timelines or inefficiencies in designing neutralizing strategies against CPV? Creative Biolabs' CPV capsid protein specific Neutra™ antibody products streamline your workflows by leveraging advanced monoclonal antibody engineering and epitope-specific validation, enabling rapid development of high-affinity neutralizing antibodies to combat CPV infections.

Introduction to CPV Capsid Protein

The canine parvovirus capsid protein (CPV capsid protein) is the principal structural component of the non-enveloped, icosahedral virion, critical for viral infectivity and host cell recognition. Comprising three viral proteins (VP1, VP2, and VP3), the capsid self-assembles into a 26 nm-diameter particle. VP2 dominates the capsid architecture, constituting ~90% of its mass, while VP1 and VP3 arise from post-translational modifications of VP2. VP2 harbors the major antigenic determinants, making it the primary target for neutralizing antibody development.

• Structural Insights

The CPV capsid exhibits a T=1 icosahedral symmetry, with 60 asymmetric VP2 trimers forming a β-barrel fold stabilized by eight antiparallel β-strands. Four surface-exposed loops (Loop1–Loop4) mediate receptor binding and antigenic specificity. Notably, the Loop2 region (residues 362–435) forms a threefold spike, directly interacting with the transferrin receptor (TfR) on host cells—a critical step for viral entry. Cryo-EM studies reveal that conformational flexibility in these loops enables immune evasion, while their conservation across parvovirus strains underscores their therapeutic targeting potential.

• Related Signaling Pathways

CPV exploits host cell endocytic pathways for internalization, facilitated by TfR binding. Post-entry, the capsid undergoes pH-dependent conformational changes to release viral DNA into the nucleus, hijacking cellular replication machinery. The capsid also interacts with innate immune sensors (e.g., TLR9), modulating interferon (IFN) responses to promote viral persistence. Neutralizing antibodies targeting VP2 disrupt these interactions, blocking viral entry and replication.

Fig.1 The molecular pathogenic mechanisms of CPV.¹

• Associated Pathologies

CPV causes severe, often fatal gastroenteritis in dogs, particularly puppies, characterized by hemorrhagic diarrhea, leukopenia, and rapid dehydration. Its high environmental stability and transmission efficiency (via fecal-oral routes) necessitate robust diagnostic and therapeutic solutions.

Applications of CPV Capsid Neutralizing Antibodies

• Vaccine Development and Efficacy Testing

Anti-CPV neutralizing antibodies serve as gold-standard reagents for quantifying vaccine-induced immune responses. By correlating antibody titers with viral neutralization capacity, researchers optimize vaccine formulations for durable immunity.

• Diagnostic Assay Development

These antibodies enable rapid, sensitive detection of CPV in clinical samples (e.g., feces or serum) via ELISA or lateral flow assays. Early diagnosis reduces mortality rates by facilitating timely therapeutic intervention.

• Therapeutic Intervention Strategies

High-affinity neutralizing antibodies are deployed in passive immunotherapy to treat acute CPV infections. Administered intravenously, they directly neutralize circulating virions, mitigate clinical symptoms, and enhance survival rates in high-risk populations.

• Antiviral Drug Discovery

Antibodies targeting VP2's receptor-binding domain are used to screen small-molecule inhibitors that mimic their neutralization mechanisms, accelerating the development of broad-spectrum parvovirus therapeutics.

Our Anti-CPV Capsid Protein Antibodies

Creative Biolabs' anti-CPV capsid antibodies are engineered to recognize conformational epitopes within VP2's hypervariable loops, ensuring precise neutralization. Key features include:

- High specificity: Validated against >20 CPV variants, including CPV-2a, -2b, and -2c.

- Cross-reactivity: Effective against feline panleukopenia virus (FPV) and mink enteritis virus (MEV).

- Functional validation: Demonstrated >95% inhibition of viral entry in in vitro neutralization assays.

Creative Biolabs delivers rigorously validated CPV capsid protein specific Neutra™ antibodies, combining unparalleled specificity with scalable production.

Contact our team today to discuss custom assay development, bulk orders, or collaborative research opportunities.

REFERENCE

1. Zhou, Hongzhuan, et al. "Overview of recent advances in canine parvovirus research: current status and future perspectives." Microorganisms 13.1 (2024): 47. Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.3390/microorganisms13010047