Showing papers by "Thomas Binz published in 1989"
TL;DR: Two monoclonal antibodies recognizing epitopes within the regions Ser-744 to Ser-864 and Ile-1224 to Asp-1315 could neutralize the toxin and a third nonneutralizing antibody was shown to recognize the synthetic peptide Phe-947 to Glu-967 derived from the tetanus toxin sequence.
Abstract: To define epitopes of tetanus toxin, we compared four different in vitro systems in terms of their ability to produce tetanus toxin-specific subfragments from cloned DNA. A transcription-translation system developed from a nontoxigenic strain of Clostridium tetani was found to yield predominantly full-sized peptides. Such peptides were used to map six different epitopes for eight monoclonal antibodies. The toxin-neutralizing properties of the antibodies were determined in an in vitro assay, based on the toxin-mediated inhibition of norepinephrine release from rat brain particles. Two monoclonal antibodies recognizing epitopes within the regions Ser-744 to Ser-864 and Ile-1224 to Asp-1315 could neutralize the toxin. A third nonneutralizing antibody was shown to recognize the synthetic peptide Phe-947 to Glu-967 derived from the tetanus toxin sequence. This peptide contains a human T-cell epitope.
12 citations
01 Jan 1989
TL;DR: Twomonoclonal antibodies recognizing epitopes within the regions Ser-744 toSer-864 andIle-1224 toAsp-1315 could neutralize the Tetanus toxin sequence, and a third nonneutralizing antibody was required toognize the synthetic peptide Phe-947 toGlu-967 derived from thetetanus toxins sequence.
Abstract: ng properties oftheantibodies weredetermined inaninvitro assay, based onthetoxin-mediated inhibition of norepinephrine release fromratbrain particles. Twomonoclonal antibodies recognizing epitopes within the regions Ser-744 toSer-864 andIle-1224 toAsp-1315 could neutralize thetoxin. A third nonneutralizing antibody wasshowntorecognize thesynthetic peptide Phe-947 toGlu-967 derived fromthetetanus toxin sequence. Thispeptide contains ahumanT-cell epitope. Tetanus toxin isahighly potent neurotoxin produced by theanaerobic bacterium Clostridium tetani. Thetoxin blocks release ofinhibitory transmitter substances from central synapses (21) after aprocess that involves binding to ganglioside receptors atthenervetermini, receptor-mediatedendocytosis, intra-axonal transport, andtranssynaptic