Year: 2011
Type: article
Abstract: Binding of pertussis toxin (PTx) was examined by glycan microarray; 53 positive hits fell into four general groups.One group represents sialylated bi-antennary compounds with an Nglycan core terminating in α2-6 linked sialic acid.The second group consists of multi-antennary compounds with an N-glycan core, but lacking terminal sialic acids, which represents a departure from previous understanding of PTx binding.The third group consists of Neu5Acα2-3Lactose that lack the branched-mannose core found in N-glycans, thus their presentation is more similar to O-glycans and glycolipids.The fourth group of compounds consists of Neu5Acα2-8Neu5Acα2-8Neu5Ac, which is seen in the c-series gangliosides and some N-glycans.Quantitative analysis by SPR of the relative affinities of PTx for terminal Neu5Acα2-3 versus Neu5Acα2-6, as well as the affinities for the trisaccharide Neu5Acα2-8Neu5Acα2-8Neu5Ac versus disaccharide, revealed identical global affinities, even though the amount of bound glycan varied by 4-to 5-fold.These studies suggest that the conformational space occupied by a glycan can play an important role in binding, independent of affinity.Characterization of N-terminal Chapter IV: Characterization of Pertussis Toxin B-Pentamer Mediated Intercellular Exchange of Plasma Membrane in Jurkat Cells.
Author: Scott H. Millen
Institution: University of Cincinnati
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
OpenAlex ID: W194762989