Abstract: An asparagine-linked glycan (N-glycan) detection reagent is provided that utilizes Fbs variants engineered from mouse Fbs proteins, wherein the Fbs variants bind specifically to N-glycosylated peptides and proteins and not to non-glycosylated peptides and proteins, including wherein the Fbs variants bind to N-glycosylated peptides and proteins and not to corresponding non-glycosylated versions of the same peptides and proteins. Compositions and methods for developing and using N-glycosylation-specific analytical, diagnostic, and therapeutic tools are provided.

Abstract: Sialic acid recognizing-affinity reagents engineered from the neuraminidase NanB have lectin-like properties and defined specificities for sialic acid.

Abstract: The carbohydrate processing enzyme PNGase F was catalytically inactivated through mutation. Additional mutations yielded a catalytically inactive carbohydrate-binding protein with lectin-like properties including high affinity and specificity N-linked glycans, O-linked glycans, or both.

Abstract: Sialic acid recognizing-affinity reagents engineered from the neuraminidase NanB have lectin-like properties and defined specificities for sialic acid.

Abstract: The carbohydrate processing enzyme PNGase F was catalytically inactivated through mutation. Additional mutations yielded a catalytically inactive carbohydrate-binding protein with lectin-like properties including high affinity and specificity N-linked glycans, O-linked glycans, or both.

Abstract: Provided are lectenz molecules, which are mutated carbohydrate processing enzyme enzymes that are catalytically inactive and that have had their substrate affinity increased by at least 1.2 fold. Further provided are methods for making and methods of using such lectenz. Further provided are compositions and methods directed to the multiplexed analysis of carbohydrates and carbohydrate containing compounds. The compositions and methods utilize suspension array technology (SAT) and an array of different carbohydrate binding molecules, each carbohydrate binding molecules with a known carbohydrate binding specificity, to obtain a glycoprofile of the carbohydrate structure(s) in a sample. Each carbohydrate binding molecule of a given specificity is linked to the external surface of a population of individually addressable particles.

Abstract: Provided are lectenz molecules, which are mutated carbohydrate processing enzymes that are catalytically inactive and that have had their substrate affinity increased by at least 1.2 fold. Further provided are methods for making and methods of using such lectenz. Additional mutated proteins following the lectenz approach are further provided.

Abstract: The carbohydrate processing enzyme PNGase F was catalytically inactivated through mutation. Additional mutations yielded a catalytically inactive carbohydrate-binding protein with lectin-like properties including high affinity and specificity N-linked glycans, O-linked glycans, or both.

Abstract: The present invention relates to novel glycomimetic compounds that are rationally designed to inhibit the binding of various pathogens to cell surface sialylated galactose and methods of use thereof. Specifically sialic acid glycosides and C-glycosides are disclosed that form a lactam ring structure or a cyclic ether/amine ring structure with the adjacent monosaccharide residue.

Abstract: The present invention relates to novel glycomimetic compounds that are rationally designed to inhibit the binding of various pathogens to cell surface sialylated galactose and methods of use thereof. Specifically sialic acid glycosides and C-glycosides are disclosed that form a lactam ring structure or a cyclic ether/amine ring structure with the adjacent monosaccharide residue.

Abstract: The present invention is includes compositions and methods directed to the multiplexed analysis of carbohydrates and carbohydrate containing compounds. The compositions and methods utilize suspension array technology (SAT) and an array of different carbohydrate binding molecules, each carbohydrate binding molecules with a known carbohydrate binding specificity, to obtain a glycoprofile of the carbohydrate structure(s) in a sample. Each carbohydrate binding molecule of a given specificity is linked to the external surface of a population of individually addressable particles.

Abstract: Provided are lectenz molecules, which are mutated carbohydrate processing enzyme enzymes that are catalytically inactive and that have had their substrate affinity increased by at least 1.2 fold. Further provided are methods for making and methods of using such lectenz. Additional mutated proteins following the lectenz approach are further provided.