Clostridium tetani TetX Specific Neutra™ Antibody Products

Are you grappling with prolonged timelines in neutralizing antibody development or inconsistent results in targeting Clostridium tetani toxins? Creative Biolabs' C. tetani TetX specific Neutra™ antibody products overcome these hurdles through advanced epitope-specific engineering and validated functional assays, empowering precise toxin neutralization and streamlined therapeutic candidate screening.

Introduction to C. tetani TetX

Clostridium tetani toxoid (C. tetani TetX) is the neurotoxic component responsible for tetanus pathogenesis. This 150 kDa protein comprises two subunits: a heavy chain (Hc) mediating neuronal receptor binding and a light chain (Lc) possessing metalloprotease activity. Upon entering the central nervous system, TetX disrupts synaptic vesicle fusion by cleaving synaptobrevin, a critical protein in neurotransmitter release.

Fig.1 Structure of the tetanus toxin molecule.¹

• Basic Information

C. tetani TetX is a zinc-dependent endopeptidase secreted during vegetative growth of C. tetani. Its high conservation across bacterial strains makes it a pivotal target for therapeutic intervention. The toxin's structure-function relationship is central to its pathogenicity, with the Hc domain binding to neuronal gangliosides (e.g., GT1b) and the Lc domain exerting proteolytic activity.

• Structural Insights

The Hc domain of TetX consists of three subdomains: a β-trefoil fold (receptor-binding site), a jelly-roll motif, and an α-helical bundle. Cryo-EM studies reveal that the Hc-Lc complex undergoes conformational rearrangement upon pH shifts in endosomes, enabling cytosolic translocation. Mutagenesis in the Hc's ganglioside-binding loop (residues 1220–1310) significantly reduces neuronal uptake.

• Related Signaling Pathways

TetX indirectly modulates host pathways by blocking inhibitory neurotransmission. Proteolytic cleavage of synaptobrevin-2 (VAMP2) disrupts SNARE complex assembly, leading to unchecked acetylcholine release at neuromuscular junctions. This hyperexcitability triggers muscle rigidity and spasms, hallmarks of clinical tetanus.

Fig.2 Proposed internalization pathway of tetanus toxin.¹

• Associated Pathology

Tetanus, a life-threatening disease, manifests as trismus (lockjaw), generalized muscle rigidity, and autonomic dysfunction. Mortality rates exceed 30% in unvaccinated populations, underscoring the urgency of neutralizing toxin activity post-exposure.

Applications of C. tetani TetX Neutralizing Antibodies

• Therapeutic Intervention

Neutralizing antibodies administered post-exposure reduce toxin dissemination to motor neurons. Clinical studies show early antibody administration correlates with decreased hospitalization duration and mortality.

• Prophylactic Strategies

High-risk populations (e.g., unvaccinated individuals) benefit from passive immunization using antibodies to prevent tetanus onset after wound contamination.

• Diagnostic Development

Antibodies enable rapid toxin detection in wound exudates or serum via lateral flow assays, facilitating timely antitoxin therapy.

• Vaccine Efficacy Evaluation

Quantifying TetX-neutralizing antibody titers in vaccinated individuals validates immune response durability, supporting vaccine lot release and adjuvant optimization.

Our Anti-C. tetani TetX Antibody Products

Creative Biolabs' TetX-specific antibodies are engineered to disrupt critical toxin functions:

- Neutralization via Hc Binding: High-affinity antibodies block ganglioside interactions, preventing neuronal internalization.

- Catalytic Inhibition: Antibodies targeting the Lc active site abrogate proteolytic activity, preserving synaptic function.

- Epitope Mapping: Our antibodies are validated against conformational epitopes in the Hc β-trefoil region, ensuring specificity.

Robust validation in in vitro neutralization assays (ED50 < 1 nM) and murine toxin challenge models demonstrates potency for therapeutic and diagnostic applications. Creative Biolabs offers C. tetani TetX-specific Neutra™ antibody portfolio that integrates cutting-edge specificity and translational relevance for tetanus research and therapeutic development.

Contact our team today to discuss custom antibody engineering, bulk production, or assay optimization.

REFERENCE

1. Calvo, Ana C., et al. "Fragment C of tetanus toxin: new insights into its neuronal signaling pathway." International journal of molecular sciences 13.6 (2012): 6883-6901. Distributed under Open Access license CC BY 3.0, without modification. https://doi.org/10.3390/ijms13066883