Carbohydrate recognition mechanism of HA70 from Clostridium botulinum deduced from X-ray structures in complexes with sialylated oligosaccharides

Satoshi Yamashita, Hiromi Yoshida, Noboru Uchiyama, Yukari Nakakita, Shin Ichi Nakakita, Takashi Tonozuka, Keiji Oguma, Atsushi Nishikawa, Shigehiro Kamitori

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)

Abstract

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

Original languageEnglish
Pages (from-to)2404-2410
Number of pages7
JournalFEBS Letters
Volume586
Issue number16
DOIs
Publication statusPublished - 2012 Jul 30

Keywords

  • Clostridium botulinum
  • Hemagglutinin
  • Sialylated oligosaccharide
  • X-ray structure

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Carbohydrate recognition mechanism of HA70 from Clostridium botulinum deduced from X-ray structures in complexes with sialylated oligosaccharides'. Together they form a unique fingerprint.

Cite this