Structure and function of Clostridium botulinum toxins.

Sakaguchi, Genji

doi:10.3412/jsb.43.951

Cited by 27 publications

(47 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…One of the reasons for this phenomenon is the protective effect of NAPs toward BoNT in the toxin complex against the low pH and proteases in the digestive tract (Sakaguchi et al, 1984). Meanwhile, the direct interaction of HA proteins with the intestinal epithelium via cell-surface glycoconjugates (Fujinaga et al, 1997(Fujinaga et al, , 2000Kojima et al, 2005;Nakamura et al, 2007) has been reported.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Disruption of the epithelial barrier by botulinum haemagglutinin (HA) proteins – differences in cell tropism and the mechanism of action between HA proteins of types A or B, and HA proteins of type C

et al. 2009

View full text Add to dashboard Cite

Orally ingested botulinum neurotoxin (BoNT) causes food-borne botulism, but BoNT must pass through the gut lining and enter the bloodstream. We have previously found that type B haemagglutinin (HA) proteins in the toxin complex play an important role in the intestinal absorption of BoNT by disrupting the paracellular barrier of the intestinal epithelium, and therefore facilitating the transepithelial delivery of BoNT. Here, we show that type A HA proteins in the toxin complex have a similar disruptive activity and a greater potency than type B HA proteins in the human intestinal epithelial cell lines Caco-2 and T84 and in the canine kidney epithelial cell line MDCK I. In contrast, type C HA proteins in the toxin complex (up to 300 nM) have no detectable effect on the paracellular barrier in these human cell lines, but do show a barrier-disrupting activity and potent cytotoxicity in MDCK I. These findings may indicate that type A and B HA proteins contribute to the development of food-borne botulism, at least in humans, by facilitating the intestinal transepithelial delivery of BoNTs, and that the relative inability of type C HA proteins to disrupt the paracellular barrier of the human intestinal epithelium is one of the reasons for the relative absence of food-borne human botulism caused by type C BoNT.

show abstract

Section: Introductionmentioning

confidence: 99%

“…1). Three different forms of progenitor toxins have been identified: 12S, 16S and 19S (Oguma et al, 1999;Sakaguchi et al, 1984). 12S toxin is composed of a BoNT and an NTNH.…”

Section: Introductionmentioning

confidence: 99%

Disruption of the epithelial barrier by botulinum haemagglutinin (HA) proteins – differences in cell tropism and the mechanism of action between HA proteins of types A or B, and HA proteins of type C

et al. 2009

View full text Add to dashboard Cite

show abstract

“…In the type A strain, three different sized progenitor toxins with molecular masses of 900 kDa (19S), 500 kDa (16S) and 300 kDa (12S) are produced. Type B, C and D strains produce both the 16S and 12S toxins, whereas the type E and F strains produce only the 12S toxin and type G strain produces only the 16S toxin (Sakaguchi et al, 1984). In all these strains, the non-toxic components of the 19S and 16S toxins display haemagglutinin (HA) activity but that of the 12S toxin does not.…”

Section: Introductionmentioning

confidence: 99%

Clostridium botulinum type A haemagglutinin-positive progenitor toxin (HA+-PTX) binds to oligosaccharides containing Galβ1-4GlcNAc through one subcomponent of haemagglutinin (HA1)

et al. 2001

View full text Add to dashboard Cite

show abstract

“…In type A, three different-sized progenitor toxins with Mr of 900 kDa (19S), 500 kDa (16S), and 300 kDa (12S) were produced. The type B, C, and D strains produce the 16S and 12S toxins, whereas types E, F, and G produce only a single form: Types E and F produce the 12S toxin and type G produces the 16S (11).…”

mentioning

confidence: 99%

Molecular Composition of the 16S Toxin Produced by a Clostridium botulinum Type D Strain, 1873

Nakajima

Inoue

Ikeda

et al. 1998

Microbiology and Immunology

View full text Add to dashboard Cite

The 16S toxin was purified from a Clostridium botulinum type D strain 1873 (D-1873). Furthermore, the entire nucleotide sequences of the genes coding for the 16S toxin were determined. It became clear that the purified D-1873 16S toxin consists of neurotoxin, nontoxic nonhemagglutinin (NTNH), and hemagglutinin (HA), and that HA consists of four subcomponents, HAL HA2, HA3a, and HA3b, the same as type D strain CB16 (D-CB16) 16S toxin. The nucleotide sequences of the nontoxic components of these two strains were also found to be identical except for several bases. However, the culture supernatant and the purified 16S toxin of D-1873 showed little HA activity, unlike D-CB16, though the fractions successively eluted after the D-1873 16S toxin peak from an SP-Toyopearl 650S column showed a low level of HA activity. The main difference between D-1873 and D-CB16 HA molecules was the mobility of the HAI. on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Therefore it was presumed that the loss of HA activity of D-1873 16S toxin might be caused by the differences of processing HA after the translation.

show abstract

Structure and function of Clostridium botulinum toxins.

Cited by 27 publications

References 0 publications

Disruption of the epithelial barrier by botulinum haemagglutinin (HA) proteins – differences in cell tropism and the mechanism of action between HA proteins of types A or B, and HA proteins of type C

Disruption of the epithelial barrier by botulinum haemagglutinin (HA) proteins – differences in cell tropism and the mechanism of action between HA proteins of types A or B, and HA proteins of type C

Clostridium botulinum type A haemagglutinin-positive progenitor toxin (HA+-PTX) binds to oligosaccharides containing Galβ1-4GlcNAc through one subcomponent of haemagglutinin (HA1)

Molecular Composition of the 16S Toxin Produced by a Clostridium botulinum Type D Strain, 1873

Contact Info

Product

Resources

About