Title of article :
Inhibition of influenza-virus-induced cytopathy by sialylglycoconjugates Original Research Article
Author/Authors :
Takashi Terabayashi، نويسنده , , Minoru Morita، نويسنده , , Masaki Ueno، نويسنده , , Tadashi Nakamura، نويسنده , , Tadasu Urashima، نويسنده ,
Issue Information :
دوهفته نامه با شماره پیاپی سال 2006
Abstract :
The anti-viral activity of gangliosides such as SPG (sialylparagloboside), GD1a, GM3, and GM4 was assessed by inhibition of the cytopathy of MDCK cells due to infection with the influenza virus A/PR/8/34. The inhibitory effect was in the following sequence: SPG > GD1a > GM3 > GM4. The IC50 of SPG and GD1a was 7 and 70 μM, respectively, indicating that they are more effective than the representative inhibitor amantadine. Although 3′-sialyllactose (3′-SL) and 3′-sialyllactosamine (3′-SLN), which are identical to the terminal trisaccharides of GM3 and SPG, respectively, did not show any inhibitory effect, introduction of an amino group to the reducing end of 3′-SL following amidation with lauroyl chloride gave the inhibitory potency, which was comparable to that of GM3. These results suggest that the viral hemagglutinin recognizes exogenous sialyloligosaccharides rather than inherent sialyloligosaccharides expressed on MDCK cells, since introduction of the hydrophobic moiety to oligosaccharides might cause micelle formation.
Keywords :
Docking , Mannosidase , Enzyme mechanism , transition state , AutoDock , Structure–function relationship , Carbohydrate conformation , GH47
Journal title :
Carbohydrate Research
Journal title :
Carbohydrate Research