Journal of Virology · 1982 · 51 citations · 17 references
Life SciencesBiochemistryMicrobiologyMolecular VirologyVaccinologyVirologyViral InfectionsViral Protein ProcessingViral ReplicationViral StructureVirus MorphologyVirus StructureCleavage-dependent Viral InfectivityHemolysis AssaysPathogen InfectivityPh DependenceViral Envelope GlycoproteinsViral Envelope ProteinsViral Fusion ProteinsViral Glycoprotein Processing
Influenza C virus showed a marked hemolytic activity when incubated with murine erythrocytes at 37 degrees C in acidic medium. The virus-specific hemolysis was most efficient at pH 5.0. Extensive cell fusion also occurred when the erythrocytes were treated with the virus at acidic pH. When propagated in MDCK cells, the virus had an extremely low infectivity and did not display hemolytic activity in any pH range. When the inactive virus was subjected to mild trypsin treatment, hemolytic activity was drastically manifested, accompanying a drastic increase in infectivity. The glycoprotein in the inactive virus was cleaved into smaller components by trypsin treatments. These results indicated that the envelope of influenza C virus can fuse with the cellular membrane under acidic conditions and that the activation of influenza C virus by cleavage was due to the appearance of this envelope fusion activity.
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