Source:http://linkedlifedata.com/resource/pubmed/id/12974634
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rdf:type | |
lifeskim:mentions |
umls-concept:C0040549,
umls-concept:C0205103,
umls-concept:C0205197,
umls-concept:C0315083,
umls-concept:C0439855,
umls-concept:C0449432,
umls-concept:C0678594,
umls-concept:C1179435,
umls-concept:C1518413,
umls-concept:C1524073,
umls-concept:C1548799,
umls-concept:C1705248,
umls-concept:C1706853,
umls-concept:C1711351,
umls-concept:C1879748
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pubmed:issue |
37
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pubmed:dateCreated |
2003-9-16
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pubmed:databankReference | |
pubmed:abstractText |
Clostridium botulinum serotype D strains usually produce two types of stable toxin complex (TC), namely, the 300 kDa M (M-TC) and the 660 kDa L (L-TC) toxin complexes. We previously proposed assembly pathways for both TCs [Kouguchi, H., et al. (2002) J. Biol. Chem. 277, 2650-2656]: M-TC is composed by association of neurotoxin (NT) and nontoxic nonhemagglutinin (NTNHA); conjugation of M-TC with three auxiliary types of hemagglutinin subcomponents (HA-33, HA-17, and HA-70) leads to the formation of L-TC. In this study, we found three TC species, 410, 540, and 610 kDa TC species, in the culture supernatant of type D strain 4947. The 540 and 610 kDa TC species displayed banding patterns on SDS-PAGE similar to that of L-TC but with less staining intensity of the HA-33 and HA-17 bands than those of L-TC, indicating that these are intermediate species in the pathway to L-TC assembly. In contrast, the 410 kDa TC species consisted of M-TC and two molecules of HA-70. All of the TC species, except L-TC, demonstrated no hemagglutination activity. When the intermediate TC species were mixed with an isolated HA-33/17 complex, every TC species converted to 650 kDa L-TC with full hemagglutination activity and had the same molecular composition of L-TC. On the basis of titration analysis with the HA-33/17 complex, the stoichiometry of the HA-33/17 complex molecules in the L-TC, 610 kDa, and 540 kDa TC species was estimated as 4, 3, and 2, respectively. In conclusion, the complete subunit composition of mature L-TC is deduced to be a dodecamer assembled by a single NT, a single NTNHA, two HA-70, four HA-33, and four HA-17 molecules.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
23
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pubmed:volume |
42
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
10991-7
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:12974634-Amino Acids,
pubmed-meshheading:12974634-Botulinum Toxins,
pubmed-meshheading:12974634-Chromatography, Gel,
pubmed-meshheading:12974634-Clostridium botulinum,
pubmed-meshheading:12974634-Dose-Response Relationship, Drug,
pubmed-meshheading:12974634-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12974634-Hemagglutination,
pubmed-meshheading:12974634-Molecular Sequence Data,
pubmed-meshheading:12974634-Protein Binding,
pubmed-meshheading:12974634-Protein Conformation,
pubmed-meshheading:12974634-Protein Structure, Tertiary
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pubmed:year |
2003
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pubmed:articleTitle |
Complete subunit structure of the Clostridium botulinum type D toxin complex via intermediate assembly with nontoxic components.
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pubmed:affiliation |
Department of Food Science and Technology, Faculty of Bioindustry, Tokyo University of Agriculture, 196 Yasaka, Abashiri 099-2493, Japan.
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pubmed:publicationType |
Journal Article
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