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Published on: June 16, 2011
Observations and implications of proteolysis in preparations of foot-and-mouth disease virus
Abstract:
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.
Insights
Foot-and-mouth disease virus VP1 protein integrity is compromised during concentration. Protein degradation reduces antibody stimulation, impacting vaccine efficacy.
Area of Science:
- Veterinary Virology
- Molecular Biology
- Immunology
Background:
- Foot-and-mouth disease virus (FMDV) is a significant global livestock pathogen.
- The viral protein 1 (VP1) is a key immunogenic component of FMDV.
- Understanding VP1 stability is crucial for vaccine development and virus characterization.
Purpose of the Study:
- To assess the integrity of the FMDV VP1 protein under different storage and concentration conditions.
- To investigate the impact of VP1 degradation on the immunogenicity of FMDV.
- To evaluate the potential of protease inhibitors in preserving VP1 stability.
Main Methods:
- Polyacrylamide gel electrophoresis (PAGE) was used to analyze VP1 protein integrity.
- FMDV preparations were stored at 4°C and subjected to concentration processes.
- Proteolytic enzyme inhibitors (Trasylol) and enzymes (trypsin) were utilized.
- Vaccination experiments in guinea pigs were conducted to assess antibody responses.
Main Results:
- VP1 degradation was minimal in tissue culture filtrates but significant in concentrated virus preparations.
- The protease inhibitor Trasylol showed potential in inhibiting VP1 degradation in some samples.
- Cleavage of FMDV VP1 by proteolytic enzymes consistently resulted in lower stimulation of neutralizing and total antibodies.
Conclusions:
- Concentration procedures can lead to significant degradation of the FMDV VP1 protein.
- VP1 degradation is associated with reduced antibody responses, suggesting impaired immunogenicity.
- Protease inhibitors may offer a strategy to maintain VP1 integrity, potentially improving vaccine effectiveness.
