TY - JOUR
T1 - Carbohydrate recognition mechanism of HA70 from Clostridium botulinum deduced from X-ray structures in complexes with sialylated oligosaccharides
AU - Yamashita, Satoshi
AU - Yoshida, Hiromi
AU - Uchiyama, Noboru
AU - Nakakita, Yukari
AU - Nakakita, Shin Ichi
AU - Tonozuka, Takashi
AU - Oguma, Keiji
AU - Nishikawa, Atsushi
AU - Kamitori, Shigehiro
N1 - Funding Information:
We thank Dr. Toshio Nakamura for helpful discussions about purification and crystallization of HA70/C. This research was supported in part by a Grant-in-Aid for Scientific Research (B) (23370054) from Japan Society for the Promotion of Science and Ministry of Education, Culture, Sports, Science and Technology of Japan, and by the fund for Characteristic Prior Research 2009–2011 from Kagawa University. This research was performed with the approval of the Photon Factory Advisory Committee and the National Laboratory for High Energy Physics (2009G512, 2010G001, 2010G582), and Priority Program for Disaster-Affected Quantum Beam Facilities of SPring-8 (2011A1873).
PY - 2012/7/30
Y1 - 2012/7/30
N2 - Clostridium botulinum produces the botulinum neurotoxin, forming a large complex as progenitor toxins in association with non-toxic non-hemagglutinin and/or several different hemagglutinin (HA) subcomponents, HA33, HA17 and HA70, which bind to carbohydrate of glycoproteins from epithelial cells in the infection process. To elucidate the carbohydrate recognition mechanism of HA70, X-ray structures of HA70 from type C toxin (HA70/C) in complexes with sialylated oligosaccharides were determined, and a binding assay by the glycoconjugate microarray was performed. These results suggested that HA70/C can recognize both α2-3- and α2-6-sialylated oligosaccharides, and that it has a higher affinity for α2-3-sialylated oligosaccharides. Crown
AB - Clostridium botulinum produces the botulinum neurotoxin, forming a large complex as progenitor toxins in association with non-toxic non-hemagglutinin and/or several different hemagglutinin (HA) subcomponents, HA33, HA17 and HA70, which bind to carbohydrate of glycoproteins from epithelial cells in the infection process. To elucidate the carbohydrate recognition mechanism of HA70, X-ray structures of HA70 from type C toxin (HA70/C) in complexes with sialylated oligosaccharides were determined, and a binding assay by the glycoconjugate microarray was performed. These results suggested that HA70/C can recognize both α2-3- and α2-6-sialylated oligosaccharides, and that it has a higher affinity for α2-3-sialylated oligosaccharides. Crown
KW - Clostridium botulinum
KW - Hemagglutinin
KW - Sialylated oligosaccharide
KW - X-ray structure
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U2 - 10.1016/j.febslet.2012.05.055
DO - 10.1016/j.febslet.2012.05.055
M3 - Article
C2 - 22684008
AN - SCOPUS:84864287475
VL - 586
SP - 2404
EP - 2410
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 16
ER -