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A mutant of Sindbis virus which is released efficiently from cells maintained in low ionic strength medium
1Department of Molecular Genetics and Microbiology, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway 08854-5635, USA.
Virology
|July 10, 1995
Summary
Researchers identified a Sindbis virus mutant resistant to low ionic strength (LIS) medium. Specific amino acid changes in the E2 protein enabled progeny virus release in LIS conditions.
Area of Science:
- Virology
- Molecular Biology
Background:
- Previous studies indicated that low ionic strength (LIS) medium inhibits Sindbis virus progeny release.
- This inhibition was hypothesized to be linked to the properties of viral envelope proteins.
Purpose of the Study:
- To investigate the role of viral envelope proteins in LIS-induced inhibition of Sindbis virus release.
- To isolate a Sindbis virus mutant resistant to LIS medium and identify the underlying genetic changes.
Main Methods:
- Isolation of a Sindbis virus mutant exhibiting resistance to LIS medium.
- Genetic analysis to identify mutations responsible for LIS resistance.
- Characterization of the identified mutations within the viral E2 protein.
Main Results:
- Successful isolation of a Sindbis virus mutant resistant to LIS medium.
- Identification of two specific amino acid substitutions (Glutamic acid at position 23 and Threonine at position 76) in the E2 protein.
- These mutations conferred the ability for infectious progeny virus release in LIS medium.
Conclusions:
- The susceptibility of Sindbis virus release to LIS inhibition is indeed determined by viral envelope protein properties.
- Specific amino acid alterations in the E2 protein can overcome LIS-mediated inhibition, enabling virus release.