Related Experiment Video
Updated: Aug 27, 2025

Affinity Purification of Influenza Virus Ribonucleoprotein Complexes from the Chromatin of Infected Cells
Published on: June 3, 2012
Functional Analysis of Sulfatide in Influenza A Virus Infection and Replication
Tadanobu Takahashi1, Yuuki Kurebayashi1, Takashi Suzuki2
1Department of Biochemistry, School of Pharmaceutical Sciences, University of Shizuoka, Shizuoka, Japan.
Abstract:
3-O-sulfation synthesizes sulfatide in the galactose moiety of galactosylceramide. Sulfatide is expressed in many organs such as the gastrointestinal tract, trachea, kidney, and central nervous system. Influenza A virus binds not only to glycoconjugates terminally containing sialic acid as a viral binding receptor but also to sulfatide not containing sialic acid. On the surface of infected cells, the envelope glycoprotein hemagglutinin of influenza A virus interacts with sulfatide. This interaction enhances the nuclear export of viral ribonucleoprotein complexes, resulting in efficient progeny viruses. Inhibiting this interaction would be a new potent anti-influenza drug that suppresses the progeny virus production in the infected cells.
More Related Videos
09:31Fluorescence-based Neuraminidase Inhibition Assay to Assess the Susceptibility of Influenza Viruses to The Neuraminidase Inhibitor Class of Antivirals
Published on: April 15, 2017
07:24In Vitro Disassembly of Influenza A Virus Capsids by Gradient Centrifugation
Published on: March 27, 2016