Abstract
Of 11 monoclonal antibodies (MAbs) prepared against the non-toxic component of type C Clostridium botulinum 16S toxin to clarify the function of the non-toxic component, seven recognised HA1, three recognised HA3b and one recognised HA2. Results of epitope mapping indicated that three of the seven anti-HA1 MAbs recognised the region between amino acid residues 121 and 140 and four recognised the three-dimensional structure of HA1. Three anti-HA3b MAbs recognised different regions between (approximately) amino acids 405-430, 180-270 and 275-297. The ability of these MAbs to interfere with binding of 16S toxin or non-toxic component, HA1 or HA3b to erythrocytes and to intestine tissue sections of guinea-pig was observed. MAbs against HA3b and HA2 did not inhibit 16S toxin binding to either erythrocytes or epithelial cells, whereas some MAbs against HA1 did inhibit binding. The seven anti-HA1 MAbs can be classified into four groups based on their binding inhibition activities. The anti-HA1 MAbs that inhibited the binding of 16S toxin to the epithelial cells also neutralised or reduced the oral toxicity in mice, indicating that HA may play an important role in the absorption of the 16S toxin from the small intestine.
| Original language | English |
|---|---|
| Pages (from-to) | 286-294 |
| Number of pages | 9 |
| Journal | Journal of Medical Microbiology |
| Volume | 51 |
| Issue number | 4 |
| Publication status | Published - 2002 |
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ASJC Scopus subject areas
- Microbiology (medical)
- Microbiology
Cite this
Characterisation of monoclonal antibodies against haemagglutinin associated with Clostridium botulinum type C neurotoxin. / Mahmut, Nazira; Inoue, Kaoru; Fujinaga, Yukako; Hughes, Lynn; Arimitsu, Hideyuki; Sakaguchi, Yoshihiko; Ohtsuka, Aiji; Murakami, Takuro; Yokota, Kenji; Oguma, Keiji.
In: Journal of Medical Microbiology, Vol. 51, No. 4, 2002, p. 286-294.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Characterisation of monoclonal antibodies against haemagglutinin associated with Clostridium botulinum type C neurotoxin
AU - Mahmut, Nazira
AU - Inoue, Kaoru
AU - Fujinaga, Yukako
AU - Hughes, Lynn
AU - Arimitsu, Hideyuki
AU - Sakaguchi, Yoshihiko
AU - Ohtsuka, Aiji
AU - Murakami, Takuro
AU - Yokota, Kenji
AU - Oguma, Keiji
PY - 2002
Y1 - 2002
N2 - Of 11 monoclonal antibodies (MAbs) prepared against the non-toxic component of type C Clostridium botulinum 16S toxin to clarify the function of the non-toxic component, seven recognised HA1, three recognised HA3b and one recognised HA2. Results of epitope mapping indicated that three of the seven anti-HA1 MAbs recognised the region between amino acid residues 121 and 140 and four recognised the three-dimensional structure of HA1. Three anti-HA3b MAbs recognised different regions between (approximately) amino acids 405-430, 180-270 and 275-297. The ability of these MAbs to interfere with binding of 16S toxin or non-toxic component, HA1 or HA3b to erythrocytes and to intestine tissue sections of guinea-pig was observed. MAbs against HA3b and HA2 did not inhibit 16S toxin binding to either erythrocytes or epithelial cells, whereas some MAbs against HA1 did inhibit binding. The seven anti-HA1 MAbs can be classified into four groups based on their binding inhibition activities. The anti-HA1 MAbs that inhibited the binding of 16S toxin to the epithelial cells also neutralised or reduced the oral toxicity in mice, indicating that HA may play an important role in the absorption of the 16S toxin from the small intestine.
AB - Of 11 monoclonal antibodies (MAbs) prepared against the non-toxic component of type C Clostridium botulinum 16S toxin to clarify the function of the non-toxic component, seven recognised HA1, three recognised HA3b and one recognised HA2. Results of epitope mapping indicated that three of the seven anti-HA1 MAbs recognised the region between amino acid residues 121 and 140 and four recognised the three-dimensional structure of HA1. Three anti-HA3b MAbs recognised different regions between (approximately) amino acids 405-430, 180-270 and 275-297. The ability of these MAbs to interfere with binding of 16S toxin or non-toxic component, HA1 or HA3b to erythrocytes and to intestine tissue sections of guinea-pig was observed. MAbs against HA3b and HA2 did not inhibit 16S toxin binding to either erythrocytes or epithelial cells, whereas some MAbs against HA1 did inhibit binding. The seven anti-HA1 MAbs can be classified into four groups based on their binding inhibition activities. The anti-HA1 MAbs that inhibited the binding of 16S toxin to the epithelial cells also neutralised or reduced the oral toxicity in mice, indicating that HA may play an important role in the absorption of the 16S toxin from the small intestine.
UR - http://www.scopus.com/inward/record.url?scp=0036201088&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036201088&partnerID=8YFLogxK
M3 - Article
C2 - 11926732
AN - SCOPUS:0036201088
VL - 51
SP - 286
EP - 294
JO - Journal of Medical Microbiology
JF - Journal of Medical Microbiology
SN - 0022-2615
IS - 4
ER -