pH-dependent hemolysis and cell fusion of rhabdoviruses.
Human erythrocytes pretreated with fungal semialkali protease or trypsin became susceptible to hemagglutination by vesicular stomatitis virus (VSV) and rabies virus. Both viruses exhibited extensive hemolytic and fusion activities against erythrocytes pretreated with these enzymes. The hemolysis and fusion were pH dependent and the activities were most apparent at pH 5.0 and decreased with increase in pH. However, VSV still exhibited slight hemolytic activity at neutral pH. Hemolysis was also dependent on the dose of virus and was inhibited by treatment of the viruses with antiviral antibody. Results of sodium dodecyl sulfate polyacrylamide gel electrophoresis of erythrocyte membranes suggested that most of the carbohydrates were removed from the membrane proteins by the treatment with proteolytic enzymes.
D000818:Animals; D000914:Antibodies, Viral; D002241:Carbohydrates / Q000502:physiology; D002459:Cell Fusion; D005777:Geese / Q000097:blood; D006387:Hemagglutination, Viral; D006461:Hemolysis; D006801:Humans; D008565:Membrane Proteins / Q000032:analysis; D010447:Peptide Hydrolases / Q000494:pharmacology; D010504:Periodic Acid / Q000494:pharmacology; D011817:Rabbits / Q000097:blood; D011820:Rabies virus / Q000502:physiology*; D013696:Temperature; D014357:Trypsin / Q000494:pharmacology; D014721:Vesicular stomatitis Indiana virus / Q000276:immunology / Q000502:physiology*
D000914:Antibodies, Viral; D002241:Carbohydrates; D008565:Membrane Proteins; D010504:Periodic Acid; C009288:metaperiodate; D010447:Peptide Hydrolases; D014357:Trypsin