Nectrisine Is a Potent Inhibitor of α-Glucosidases, Demonstrating Activities Similarly at Enzyme and Cellular Levels

• Published in: Biochemical and biophysical research communications Vol. 220; no. 2; pp. 459 - 466
• Main Authors: Tsujii, Eisaku, Muroi, Makoto, Shiragami, Nobue, Takatsuki, Akira
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 18.03.1996
• Subjects: 1-Deoxynojirimycin - pharmacology; Acetylglucosaminidase - antagonists & inhibitors; Adjuvants, Immunologic; alpha-Mannosidase; Animals; beta-Glucosidase - antagonists & inhibitors; beta-Mannosidase; Cell Line; Cricetinae; Enzyme Inhibitors - pharmacology; Giant Cells - drug effects; Glycoproteins - metabolism; Glycoside Hydrolase Inhibitors; HN Protein - biosynthesis; Imino Furanoses; Indolizines - pharmacology; Mannosidases - antagonists & inhibitors; Pyrrolidines - pharmacology; Rats
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1996.0427

Nectrisine, discovered as an immunomodulator, was found to inhibit α-glucosidase, α- and β-mannosidases, β-glucosidase and β-N-acetylglucosaminidase, in that order of inhibition strength. β-Galactosidase, α-fucosidase, and neuraminidase were insensitive to this antibiotic. Also sensitive was the trimming glucosidase I which participates in the first step of modifyingN-glycosidic oligosaccharide. Nectrisine demonstrated an inhibitory effect at the cellular level as strong as expected based on its action at enzyme levels; castanospermine and 1-deoxynojirimycin did not. Nectrisine and castanospermine suppressed syncytium formation and hemolytic activity in Newcastle disease virus (NDV)-infected BHK cells, without blocking the synthesis and cell-surface expression of HANA glycoprotein of NDV.