Glycoconjugate journal special issue on: the glycobiology of Parkinson's disease.

Parkinson's disease (PD) is a neurodegenerative disorder that affects over 10 million aging people worldwide. This condition is characterized by the degeneration of dopaminergic neurons in the pars compacta region of the substantia nigra (SNpc) and by aggregation of proteins, commonly α-synuclein (SNCA). The formation of Lewy bodies that encapsulate aggregated proteins in lipid vesicles is a hallmark of PD.

Biochemical characterization of WbdN, a β1,3-glucosyltransferase involved in O-antigen synthesis in enterohemorrhagic Escherichia coli O157.

The enterohemorrhagic O157 strain of Escherichia coli, which is one of the most well-known bacterial pathogens, has an O-antigen repeating unit structure with the sequence [-2-d-Rha4NAcα1-3-l-Fucα1-4-d-Glcβ1-3-d-GalNAcα1-]. The O-antigen gene cluster of E. coli O157 contains the genes responsible for the assembly of this repeating unit and includes wbdN.

Inhibition of glycosyltransferase activities as the basis for drug development.

Glycosyltransferases are involved in the biosynthesis of protein-bound glycan chains that have multiple and important biological functions in all species. In this protocol, we describe methods to assess the inhibition of glycosyltransferase activities. The kinetic mechanisms of the enzymes, information from structural studies and preliminary inhibition studies can aid in designing appropriate inhibitors.

Synthesis of cell envelope glycoproteins of Cryptococcus laurentii.

Fungi of the genus Cryptococcus are encapsulated basidiomycetes that are ubiquitously found in the environment. These organisms infect both lower and higher animals. Human infections that are common in immune-compromised individuals have proven difficult to cure or even control with currently available antimycotics that are quite often toxic to the host.

Assay of dolichyl-phospho-mannose synthase reconstituted in a lipid matrix.

Advances in molecular biology over the last several decades, along with new highly developed methods for protein expression, have enabled investigators to produce and purify large yields of the soluble protein domains of a number of eukaryotic glycosyltransferases and processing glycosidases. The availability of these purified enzymes has in turn allowed determination of the crystal structures of the catalytic domains of some of the proteins, thus providing details of the active site geometry and catalytic mechanisms of the enzymes. It must be remembered, however, that the natural subcellular locations for enzymes involved in glycoprotein and glycolipid synthesis are the membranes of the endoplasmic reticulum and Golgi, where the enzymes exist bound to or inserted in the membrane matrix.