4en9
From Proteopedia
Crystal structure of HA70 (HA3) subcomponent of Clostridium botulinum type C progenitor toxin in complex with alpha 2-6-sialyllactosamine
Structural highlights
FunctionHA70C_CBCP The hemagglutinin (HA) component of the progenitor toxin protects the structural integrity of botulinum neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host (PubMed:9421908). The HA component is involved in binding to the upper small intestine through interactions with glycolipids and glycoproteins containing sialic acid moieties (Probable). Whole protein and the HA-53 chain (but not the HA-22-23 chain) bind to bovine mucin; if the mucin is pretreated with neuraminidase (removes the terminal sialic acid of glycoconjugates) mucin binding is decreased (PubMed:19071137). Has higher affinity for alpha-2,3-sialylated oligosaccharides than alpha-2-6 sialylated oligosaccharides (PubMed:22684008).[1] [2] [3] [4] Publication Abstract from PubMedClostridium 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 alpha2-3- and alpha2-6-sialylated oligosaccharides, and that it has a higher affinity for alpha2-3-sialylated oligosaccharides. Carbohydrate recognition mechanism of HA70 from Clostridium botulinum deduced from X-ray structures in complexes with sialylated oligosaccharides.,Yamashita S, Yoshida H, Uchiyama N, Nakakita Y, Nakakita S, Tonozuka T, Oguma K, Nishikawa A, Kamitori S FEBS Lett. 2012 Jul 30;586(16):2404-10. doi: 10.1016/j.febslet.2012.05.055. Epub , 2012 Jun 7. PMID:22684008[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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