Glycan–Receptor Interaction 2018

Dear Colleagues,

Cell surface carbohydrates attached to proteins and lipids are major components of the outer surface of mammalian cells. Changes to the surface glycosylation are important means of cell–cell interaction in fertilization, development, differentiation, growth, aging, adhesion, signal transduction, neurotransduction, immune systems, and carcinogenesis, metastasis, and angiogenesis. Therefore, surface glycosylations are mainly located on the borders of cells to communicate through face-to-face recognition or carbohydrate glycan–receptor interaction. Because the glycans communicate with their counterparts, such as specific receptors through purely physical interactions, the synthesis and distribution of these components are under strict genetic control. These glycosylated proteins and lipids have been implicated in multicellular functional expression and society formation, which depends on cell type, tissue type, and organ type. Modifications of cellular glycosylation are also a common phenotypic change in malignancy, with a poor prognosis for the patients. Most of the carbohydrate tumor antigens are sialylated. As examples, the mucin-type Sialyl-Tn, Sialyl-Lewis X, and Sialyl-Lewis A antigens are increased in the N-linked and O-linked oligosaccharides of the carcinoma cell glycoproteins of cancers. In recent viral pandemics, it was recognized that human and avian influenza viruses bind sialic acid-based receptors. For example, a human-type is NeuAcα2-6Gal, while an avian-type is NeuAcα2-3Gal. From the recent human type H3N2 virus, the evolutionary transition has been suggested in sialyl ligand–receptor interaction. Therefore, interaction between the influenza virus and sialic acid receptors is the hot issue of current glycan–receptor interaction. The changed glycans can regulate carbohydrate–carbohydrate, carbohydrate–protein, and carbohydrate–lipid interactions. Therefore, each glycan structure has been implicated as a face or signature of certain biological states in cells and organs. In tumors, the glycosylated antigens can be used as tumor markers for human cancer patients, especially for node-negative patients.

We invite researchers to contribute original and review articles regarding the interactions between glycans and proteins. Potential topics include, but are not limited to:

• Glycosylation of N-/O-glycoproteins
• Sialylation of glycoproteins and glycolipids
• Lectin–glycan interaction
• Sialyltransferases
• Glycosylation in malignancy and cancers
• Xenoantigenic glycosylation in non-human mammals
• Sphingolipids in membranes
• ER-specific glycobiology
• Golgy-specific glycobiology
• Glycan-based cell differentiation and development
• Glycan antigens in stem cells
• Sialyl antigen–Lectin, Galectin, Siglec
• Sugar–receptor interaction
• Innate immunity
• Xenotransplantation
• Influenza virus and sialic acid receptors
• Sialic acids mimetics as drug design

Prof. Dr. Cheorl-Ho Kim
Guest Editor

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