@article{kozaki_kamata_nishiki_kakinuma_maruyama_takahashi_karasawa_yamakawa_nakamura_1998, 
  title={Characterization of Clostridium botulinum Type B Neurotoxin Associated with Infant Botulism in Japan}, 
  volume={66}, 
  DOI={10.1128/iai.66.10.4811-4816.1998}, 
  abstractNote={<jats:p>The neurotoxin of strain 111 (111/NT) associated with type B infant botulism showed antigenic and biological properties different from that (Okra/NT) produced by a food-borne botulism-related strain, Okra. The specific toxicity of 111/NT was found to be about 10 times lower than that of Okra/NT. The monoclonal antibodies recognizing the light chain cross-reacted with both neurotoxins, whereas most of the antibodies recognizing the carboxyl-terminal half of the heavy chain of Okra/NT did not react to 111/NT. Binding experiments with rat brain synaptosomes revealed that <jats:sup>125</jats:sup>I-labeled 111/NT bound to a single binding site with a dissociation constant (<jats:italic>K<jats:sub>d</jats:sub>
                  </jats:italic>) of 2.5 nM; the value was rather lower than that (0.42 nM) of <jats:sup>125</jats:sup>I-Okra/NT for the high-affinity binding site. In the lipid vesicles reconstituted with ganglioside GT1b, <jats:sup>125</jats:sup>I-Okra/NT interacted with the amino-terminal domain of synaptotagmin 1 (Stg1N) or synaptotagmin 2 (Stg2N), fused with the maltose-binding protein, in the same manner as the respective full-length synaptotagmins, and the <jats:italic>K<jats:sub>d</jats:sub>
                  </jats:italic> values accorded with those of the low- and high-affinity binding sites in synaptosomes. However, <jats:sup>125</jats:sup>I-111/NT only exhibited a low capacity for binding to the lipid vesicles containing Stg2N, but not Stg1N, in the presence of ganglioside GT1b. Moreover, synaptobrevin-2, an intracellular target protein, was digested to the same extent by the light chains of both neurotoxins in a concentration-dependent manner. These findings indicate that the 111/NT molecule possesses the receptor-recognition site structurally different from Okra/NT, probably causing a decreased specific toxicity.</jats:p>}, 
  number={10}, 
  publisher={American Society for Microbiology}, 
  author={Kozaki, Shunji and Kamata, Yoichi and Nishiki, Tei-ichi and Kakinuma, Hiroaki and Maruyama, Hiromi and Takahashi, Hiroaki and Karasawa, Tadahiro and Yamakawa, Kiyotaka and Nakamura, Shinichi}, 
  editor={Barbieri, J. T.}, 
  year={1998}
  }