Literature DB >> 40973

Structure of tetanus toxin. Demonstration and separation of a specific enzyme converting intracellular tetanus toxin to the extracellular form.

T B Helting, S Parschat, H Engelhardt.   

Abstract

Protease activity has been demonstrated in culture supernatants of Clostridium tetani at various stages of fermentation. Gel chromatography of the concentrated filtrates revealed the presence of three enzymatically active fractions eluting at separate positions off the column. The smallest protease was found to "nick" the single chain intracellular tetanus toxin, producing the extracellular, two-chain structure of the molecule. As little as 3 ng of active protease were sufficient to cleave 50 microgram of intracellular tetanus toxin, suggesting that this enzyme is responsible for the observed structural change of the toxin molecule during its release into the culture medium. By comparison, the second protease, eluting at an intermediate position, exhibited only marginal activity towards intracellular toxin. The third, largest, enzyme was not active under the conditions of the assay. However, the latter protease effectively hydrolyzed low molecular weight histidyl peptides, and it is concluded that this enzyme is similar to the one described by Miller, P.A. Gray, C.T., and Eaton, M.D. (1960) J. Bacteriol. 79, 95-102. The properties of the partially purified enzymes, including their differential behavior towards a number of protease inhibitors, are reported.

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Year:  1979        PMID: 40973

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  11 in total

1.  Synthesis of tetanus toxin fragment C in insect cells by use of a baculovirus expression system.

Authors:  I G Charles; B C Rodgers; A J Makoff; S N Chatfield; D E Slater; N F Fairweather
Journal:  Infect Immun       Date:  1991-05       Impact factor: 3.441

2.  Limited proteolysis of single-chain tetanus toxin by tissue enzymes, in cultured brain tissue and during retrograde axonal to the spinal cord.

Authors:  E Habermann; U Weller; M Hudel
Journal:  Naunyn Schmiedebergs Arch Pharmacol       Date:  1991-03       Impact factor: 3.000

Review 3.  Properties and use of botulinum toxin and other microbial neurotoxins in medicine.

Authors:  E J Schantz; E A Johnson
Journal:  Microbiol Rev       Date:  1992-03

4.  Tetanus toxin: biochemical and pharmacological comparison between its protoxin and some isotoxins obtained by limited proteolysis.

Authors:  U Weller; F Mauler; E Habermann
Journal:  Naunyn Schmiedebergs Arch Pharmacol       Date:  1988-08       Impact factor: 3.000

5.  Cloning and expression of functional fragment C of tetanus toxin.

Authors:  J L Halpern; W H Habig; E A Neale; S Stibitz
Journal:  Infect Immun       Date:  1990-04       Impact factor: 3.441

6.  Enzymatic hydrolysis of tetanus toxin by intrinsic and extrinsic proteases. Characterization of the fragments by monoclonal antibodies.

Authors:  K Goretzki; E Habermann
Journal:  Med Microbiol Immunol       Date:  1985       Impact factor: 3.402

7.  Antibodies against the light chain of tetanus toxin in human sera.

Authors:  C S Lin; W H Habig; M C Hardegree
Journal:  Infect Immun       Date:  1985-07       Impact factor: 3.441

Review 8.  Proteolytic activation of bacterial toxins: role of bacterial and host cell proteases.

Authors:  V M Gordon; S H Leppla
Journal:  Infect Immun       Date:  1994-02       Impact factor: 3.441

9.  Pore formation by tetanus toxin, its chain and fragments in neuronal membranes and evaluation of the underlying motifs in the structure of the toxin molecule.

Authors:  J Beise; J Hahnen; B Andersen-Beckh; F Dreyer
Journal:  Naunyn Schmiedebergs Arch Pharmacol       Date:  1994-01       Impact factor: 3.000

10.  A review of the molecular structure of tetanus toxin.

Authors:  J P Robinson; J H Hash
Journal:  Mol Cell Biochem       Date:  1982-10-01       Impact factor: 3.396

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