Observations and implications of proteolysis in preparations of foot-and-mouth disease virus.
The integrity of the VP1 protein of foot-and-mouth disease virus was assessed by polyacrylamide gel electrophoresis (following storage at 4 degrees C of conventional tissue culture preparations and concentrated preparations of the virus. There was little evidence of VP1 degradation in tissue culture filtrates whereas considerable degradation was observed throughout a range of different concentrates. The use of the proteolytic enzyme inhibitor 'Trasylol' appeared to inhibit VP1 degradation in some virus preparations. Vaccination experiments with guinea pigs indicate that cleavage of O BFS 1860 virus by a range of proteolytic enzymes was always associated with a lowered stimulation of neutralising antibody and total antibody. Experiments with six other strains treated with trypsin gave similar results to those obtained with O BFS 1860.
D005537:Aphthovirus / Q000502:physiology*; D046508:Culture Techniques / Q000379:methods; D004355:Drug Stability; D004591:Electrophoresis, Polyacrylamide Gel; D010447:Peptide Hydrolases / Q000378:metabolism; D014764:Viral Proteins / Q000032:analysis*; D015678:Viral Structural Proteins
D014764:Viral Proteins; D015678:Viral Structural Proteins; D010447:Peptide Hydrolases