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Effect of undiluted passage on the polypeptides of measles virus
Abstract:
Measles virus induces a large polypeptide (L; mol. wt. 180 K), a large glycopolypeptide (H; mol. wt. 80 K), a nucleocapsid associated polypeptide (P; mol. wt. 70 K), a nucleocapsid polypeptide (N; mol. wt. 60 K), a second glycopolypeptide (F0; mol. wt. 60 K), a matrix or membrane polypeptide (M; mol. wt. 37 K) and a small polypeptide (S; mol. wt. 15 K). The second glycopolypeptide (F0) appears to be cleaved in purified measles virus. Defective interfering particles accumulate during passage of measles virus leading to a decrease in the amounts of virus-specific protein synthesized in infected cells. Even in the best preparations of purified measles virus, host proteins are always detected and these become more predominant in preparations with low infectivity.
Insights
Measles virus produces several proteins, including large polypeptides L and H, and smaller proteins like N, P, F0, M, and S. Viral passage leads to defective particles and reduced virus protein synthesis, with host proteins often contaminating purified virus preparations.
Area of Science:
- Virology
- Molecular Biology
- Protein Chemistry
Background:
- Measles virus is a significant human pathogen.
- Understanding measles virus protein composition is crucial for vaccine development and antiviral strategies.
- Previous studies have identified several viral proteins, but their precise roles and interactions require further elucidation.
Purpose of the Study:
- To characterize the polypeptide composition of measles virus.
- To investigate the effect of viral passage on protein synthesis.
- To assess the purity of measles virus preparations.
Main Methods:
- Analysis of measles virus-infected cells and purified virus preparations.
- Identification and molecular weight determination of viral polypeptides.
- Assessment of host protein contamination in purified virus.
Main Results:
- Identified seven measles virus-specific polypeptides: L (180 K), H (80 K), P (70 K), N (60 K), F0 (60 K), M (37 K), and S (15 K).
- Observed cleavage of the F0 glycopolypeptide in purified measles virus.
- Demonstrated accumulation of defective interfering particles during measles virus passage, correlating with decreased virus-specific protein synthesis.
- Consistently detected host proteins in purified measles virus, with increased prevalence in less infectious preparations.
Conclusions:
- Measles virus encodes a complex set of structural proteins.
- Viral passage and purification methods can impact viral protein synthesis and purity.
- Host protein contamination is a common issue in purified measles virus preparations, potentially affecting infectivity studies.