Escherichia coli Flagellin Specific Neutra™ Antibody Products

Are you struggling with inconsistent results in bacterial infection models or facing roadblocks in developing neutralizing antibodies against highly immunogenic targets? Creative Biolabs' E. coli flagellin specific Neutra™ antibody products leverage advanced hybridoma screening and epitope-specific engineering to deliver high-affinity antibodies, enabling accurate detection of flagellin-mediated immune responses and accelerating therapeutic development.

Introduction to E. coli Flagellin

Escherichia coli O157:H7 str. EDL933 Flagellin (E. coli Flagellin) is the primary structural protein of bacterial flagella, critical for motility and host colonization. As a pathogen-associated molecular pattern (PAMP), it binds to Toll-like receptor 5 (TLR5) and inflammasome NLRC4, triggering innate immune responses. Flagellin's conserved N- and C-terminal domains facilitate robust antibody recognition, while its hypervariable central region enables serotype specificity.

• Structural Insights

E. coli flagellin adopts a helical filament structure composed of ~500 amino acid subunits arranged in a protofilament. The protein features two conserved terminal domains (D0 and D1) essential for polymerization, flanking a hypervariable D2 domain. Cryo-EM studies reveal that TLR5 interaction occurs via conserved residues in D1, making this region a prime target for neutralizing antibodies. Structural plasticity in the D2 domain allows immune evasion in pathogenic strains, underscoring the need for antibodies targeting invariant epitopes.

• Related Signaling Pathways

Flagellin activates TLR5, initiating NF-κB and MAPK pathways to induce pro-inflammatory cytokines (e.g., IL-8, TNF-α). Simultaneously, cytosolic NLRC4 inflammasome activation drives caspase-1-mediated pyroptosis, amplifying inflammation. Persistent TLR5 signaling exacerbates conditions like sepsis, while dysregulated inflammasome activity contributes to tissue damage in gastrointestinal infections. Targeting these pathways with neutralizing antibodies can mitigate pathogenic hyperinflammation.

Fig.1 Flagellin recognition by the host.1

• Pathological Relevance

E. coli flagellin is a virulence factor in enteropathogenic (EHEC), enteroaggregative (EAEC), and uropathogenic (UPEC) E. coli strains. Infections cause hemorrhagic colitis, hemolytic uremic syndrome (HUS), and urinary tract infections. Its role in biofilm formation and immune evasion makes it a critical therapeutic target for antibiotic-resistant infections.

Applications of Anti-E. coli Flagellin Neutralizing Antibodies

• Therapeutic Intervention in Bacterial Infections

Neutralizing antibodies diminish bacterial motility and biofilm formation, enhancing antibiotic efficacy. In preclinical trials, co-administration with drug reduced EHEC colonization in gut mucosa by 70%, highlighting potential for adjunctive therapy in multidrug-resistant infections.

• Diagnostic Biomarker Detection

High-specificity antibodies enable rapid flagellin detection in stool or urine samples, aiding early diagnosis of E. coli infections. Lateral flow assays using these antibodies achieve 99% specificity in differentiating pathogenic from non-pathogenic strains, critical for outbreak management.

• Vaccine Adjuvant Development

Flagellin's intrinsic adjuvant properties are harnessed in subunit vaccines. Anti-flagellin antibodies monitor antigen stability during vaccine formulation, ensuring consistent TLR5 activation for robust adaptive immunity.

• Inflammatory Disease Research

Antibodies neutralize flagellin-induced TLR5 signaling in conditions like Crohn's disease, where bacterial translocation exacerbates inflammation. In vitro studies show reduced IL-1β and IL-18 secretion in patient-derived macrophages, suggesting therapeutic potential for immune-mediated disorders.

Our Anti- E. coli Flagellin Antibody Products

Creative Biolabs' antibodies target conformational epitopes in the TLR5-binding D1 domain, blocking receptor interaction without cross-reacting with commensal bacterial flagellins. Validated in neutralization assays, these antibodies inhibit IL-8 secretion in human intestinal epithelial cells by >90% and reduce bacterial load in murine infection models. Applications extend to quantifying flagellin in clinical samples (sensitivity <0.1 ng/mL) and studying host-pathogen interactions in real-time imaging.

Creative Biolabs offers E. coli flagellin specific Neutra™ antibody products that are engineered for unparalleled specificity and reproducibility in research and diagnostics.

Contact our team today to discuss custom antibody development or explore our catalog.

REFERENCE

1. Nedeljković, Marko, Diego Emiliano Sastre, and Eric John Sundberg. "Bacterial flagellar filament: a supramolecular multifunctional nanostructure." International Journal of Molecular Sciences 22.14 (2021): 7521. Distributed under Open Access license CC BY 4.0, without modification. https://doi.org/10.3390/ijms22147521