Struggling with prolonged timelines in allergy drug discovery or inconsistent results in IgE-mediated hypersensitivity studies? Creative Biolabs' P. avium PRUA1 specific Neutra™ antibodies deliver precise, high-affinity targeting through advanced phage display and epitope-specific engineering, enabling rapid validation of therapeutic candidates and robust diagnostic assay development.
Prunus avium major allergen Pru av 1 (P. avium PRUA1) is a pathogenesis-related class 10 (PR-10) protein and a primary allergenic trigger in cherry fruit. Expressed abundantly in pollen and fruit tissues, this 17 kDa Bet v 1-homologous protein cross-reacts with birch pollen allergens, driving IgE-mediated hypersensitivity in susceptible populations. Its role as a pan-allergen makes it a critical target for allergy diagnostics and immunotherapies.
P. avium PRUA1 adopts a conserved seven-stranded β-sheet structure flanked by two α-helices, forming a hydrophobic pocket that binds phytosteroids and other ligands. This ligand-binding domain is critical for allergenic epitope presentation. Structural plasticity at the C-terminal loop enhances immune evasion by allowing conformational masking of IgE-binding regions. Cryo-EM studies reveal that isoform-specific residues (e.g., Glu45, Asp69) govern cross-reactivity with Bet v 1, while N-glycosylation at Asn28 modulates dendritic cell recognition and Th2 polarization.
Fig.1 Three-dimensional structures of Pru av 1.1
P. avium PRUA1 activates type 2 immune responses via IL-4/IL-13 secretion, driven by protease-activated receptor 2 (PAR-2)-dependent dendritic cell maturation. The allergen's ligand-binding capacity further amplifies mast cell degranulation through FcεRI-mediated IgE cross-linking. Additionally, PRUA1 disrupts epithelial barrier integrity by downregulating occludin and claudin-5, potentiating systemic sensitization.
PRUA1 is clinically linked to oral allergy syndrome (OAS), allergic rhinitis, and asthma exacerbations. Sensitized individuals exhibit IgE cross-reactivity to stone fruits, nuts, and birch pollen, complicating diagnosis and therapeutic stratification. Severe cases progress to anaphylaxis, underscoring the urgency of developing PRUA1-specific neutralizing tools.
Anti-PRUA1 antibodies enable quantification of allergen-specific IgE in serum, distinguishing genuine PRUA1 sensitization from cross-reactive responses. This specificity reduces false positives in multiplex allergen panels, streamlining patient-specific management plans.
Neutralizing antibodies serve as blueprints for epitope-focused immunotherapies. By identifying non-anaphylactic PRUA1 epitopes, researchers engineer hypoallergenic variants for subcutaneous immunotherapy (SCIT), reducing adverse reactions during desensitization.
Monoclonal anti-PRUA1 antibodies inhibit mast cell degranulation in vitro and in murine models, demonstrating potential for rapid-onset biologics to treat OAS and prevent anaphylaxis. Early-phase trials highlight dose-dependent suppression of skin prick test reactivity.
PRUA1-specific antibodies assess vaccine efficacy by measuring IgG4 blocking activity in serum post-immunization. High-throughput IgG4/IgE ratio analysis accelerates adjuvant selection for next-generation allergy vaccines.
Creative Biolabs' anti-PRUA1 neutralizing antibodies are engineered to block IgE binding and inhibit mast cell activation. Key features include:
Applications span IgE quantification, basophil activation tests, and epitope mapping for hypoallergen design.
Creative Biolabs provides P. avium PRUA1 specific Neutra™ antibodies with unparalleled specificity for advancing allergy diagnostics and immunotherapies. Engineered to overcome cross-reactivity and enhance stability, these tools empower researchers to decode PRUA1-driven pathologies and accelerate therapeutic translation.
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Recombinant Anti-P. avium PRUA1 (N29) Antibody (V3S-0522-YC4749) (CAT#: V3S-0522-YC4749)
Target: P. avium PRUA1
Host Species: Mouse
Target Species: Prunus avium,
Application: ELISA,