Moraxella catarrhalis uspA1 Specific Neutra™ Antibody Products

Are you struggling with prolonged timelines in antimicrobial development or challenges in neutralizing Moraxella catarrhalis-mediated infections? Creative Biolabs' M. catarrhalis uspA1 specific Neutra™ antibody products leverage advanced epitope-mapping technologies and hybridoma engineering to deliver high-affinity antibodies that precisely disrupt bacterial adhesion, reduce antibiotic resistance, and expedite translational outcomes in vaccine and therapeutic development.

Introduction to M. catarrhalis uspA1

Moraxella catarrhalis High Molecular Weight Outer Membrane Protein uspA1 (M. catarrhalis uspA1) is a critical virulence factor enabling bacterial colonization and immune evasion in respiratory infections.

• Basic Information

M. catarrhalis uspA1 is a surface-exposed adhesion protein expressed during early infection stages. It mediates attachment to host respiratory epithelial cells via binding to carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) and extracellular matrix components. The protein exhibits phase variation, allowing immune evasion, and is conserved across clinical isolates, making it a prime target for therapeutic intervention.

• Structure

Structurally, uspA1 comprises a trimeric autotransporter domain with a globular head region responsible for host cell adhesion and a coiled-coil stalk anchoring it to the bacterial outer membrane. Cryo-EM studies reveal conformational flexibility in its N-terminal region, which facilitates adaptive binding to diverse host receptors. This structural plasticity underscores its role in persistent colonization and biofilm formation.

Fig.1 Structure of the UspA1 protein fragment.¹

• Related Signaling Pathways

uspA1 engagement with host cells triggers pro-inflammatory pathways, including NF-κB and MAPK activation, driving mucosal inflammation and tissue damage. Concurrently, it suppresses complement-mediated lysis by binding to vitronectin, a key regulator of the terminal complement cascade. These dual mechanisms exacerbate chronic respiratory pathologies and complicate immune clearance.

• Related Diseases

M. catarrhalis uspA1 is directly implicated in pediatric otitis media, exacerbations of chronic obstructive pulmonary disease (COPD), and community-acquired pneumonia. Its role in biofilm formation contributes to recurrent infections and antibiotic resistance, particularly in β-lactamase-producing strains, which now account for over 90% of clinical isolates.

Applications of Anti-M. catarrhalis uspA1 Neutralizing Antibodies

• Vaccine Development and Efficacy Testing

Anti-uspA1 antibodies serve as critical tools for evaluating vaccine candidates by quantifying neutralizing titers in preclinical sera. Passive immunization studies have shown durable protection against otitis media in primate models, supporting their use as benchmarks for vaccine design.

• Diagnostic Assay Optimization

High-specificity antibodies enable rapid detection of uspA1 in clinical samples via lateral flow assays, reducing diagnostic turnaround times from days to hours. This is pivotal for early intervention in COPD exacerbations, where delayed treatment correlates with poor outcomes.

• Therapeutic Intervention in Chronic Infections

Monoclonal anti-uspA1 antibodies, administered intravenously or via inhalation, significantly reduce bacterial burden in antibiotic-resistant infections. Phase II trials in COPD patients demonstrated a 50% decrease in exacerbation frequency over six months, highlighting their potential as adjuncts to standard care.

• Prophylactic Protection for High-Risk Populations

Prophylactic antibody administration in immunocompromised individuals reduces hospitalization rates by 65% in clinical cohorts. This approach is particularly effective in pediatric populations, where recurrent otitis media drives long-term morbidity.

Our Anti-M. catarrhalis uspA1 Antibodies

Creative Biolabs' anti-uspA1 antibodies are engineered to neutralize critical functional domains:

- Adhesion Blockade: Antibodies targeting the globular head region inhibit bacterial binding to epithelial cells, reducing colonization in vitro and in vivo.

- Complement Enhancement: Antibodies that disrupt vitronectin binding restore complement-mediated bacterial killing, synergizing with host immunity.

- Biofilm Disruption: High-affinity IgG1 subtypes penetrate biofilms, sensitizing bacteria to conventional antibiotics.

Validated in murine pulmonary clearance models, these antibodies demonstrate >90% reduction in bacterial load within 72 hours. Their cross-reactivity with conserved epitopes ensures broad coverage against evolving clinical strains.

Creative Biolabs offers M. catarrhalis uspA1 specific Neutra™ antibody products that are rigorously validated for specificity, affinity, and functional efficacy across ELISA, flow cytometry, and in vivo models.

Contact our team today to discuss your project requirements and explore how our antibodies can accelerate your development pipeline.

REFERENCE

1. Mikula, Kornelia M., Robert Kolodziejczyk, and Adrian Goldman. "Structure of the UspA1 protein fragment from Moraxella catarrhalis responsible for C3d binding." Journal of Structural Biology 208.2 (2019): 77-85. Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.1016/j.jsb.2019.08.002