TETANUS TOXOID, RECOMBINANT HEAVY CHAIN FRAGMENT C

Tetanus toxoid, recombinant heavy chain fragment C is a recombinant protein that is devoid of the toxin’s enzymatic activity but contains the binding site necessary for uptake of the toxin by neurons, and is the most immunogenic part of the toxin. Fragment C contains the powerful T cell epitopes of tetanus toxin without the toxicity.

PRODUCT DETAILS – TETANUS TOXOID, RECOMBINANT HEAVY CHAIN FRAGMENT C

• Carboxyl fragment of tetanus toxin heavy chain expressed in the cytoplasm of E. coli as a properly-folded, soluble protein.
• Purified in 20mM HEPES, l00mM NaCl, 10% glycerol, pH7.2.
• Manufactured to >98% purity by SEC HPLC.

BACKGROUND

TT heavy chain fragment is the C terminal fragment of the toxin (Helting & Zwisler, 1977). It is devoid of the toxin’s enzymatic activity but contains the binding site necessary for uptake of the toxin by neurons (Roux et al., 2015; Sinha et al., 2000) and is the most immunogenic part of the toxin (Ramakrishnan et al., 2015). Fragment C contains the powerful T cell epitopes of tetanus toxin without the toxicity.

Tetanus toxoid (TT) is frequently used as a carrier protein for conjugate vaccines, in addition to being a component of the DPT vaccine. TT contains strong T cell epitopes. However, as a toxoided protein, many of the surface lysines are blocked by the toxoiding process. Furthermore, TT is not a uniform product, since each manufacturer has its own specific toxoiding and purification process. Tetanus toxoid also tends to aggregate with age and is not generally affordable in the quantities needed for research and early clinical work. Recombinant TT combines the advantages of the toxoid with the reproducibility of a recombinant protein.

REFERENCES

• Helting and Zwisler. (1977). Structure of Tetanus Toxin: I. Breakdown of the Toxin Molecule. J Biol. Chem. 252:137, 1977.
• Roux et al. (2005). C-terminal fragment of tetanus toxin: its use in neuronal network analysis and its potential as non-viral vector. J Soc Biol. 199:35, 2005.
• Sinha et al. (2000). Analysis of mutants of tetanus toxin Hc fragment: ganglioside binding, cell binding and retrograde axonal transport properties. Mol Microbiol. 37:1041, 2000.
• Ramakrishnan et al. (2015). Utility of recombinant fragment C for assessment of anti-tetanus antibodies in plasma. Diagn Microbiol Infect Dis. 82:11, 2015.