Mutational analysis of the capsid protein of Leishmania RNA virus LRV1-4
| Autor: | Jean L. Patterson, Tamarra L. Cadd, Kyle J. MacBeth, Dierdre Furlong |
|---|---|
| Rok vydání: | 1994 |
| Předmět: |
viruses
Immunology Mutant Molecular Sequence Data Restriction Mapping Microbiology Polymerase Chain Reaction Open Reading Frames Capsid Virology Animals RNA Viruses Cloning Molecular DNA Primers Sequence Deletion Electrophoresis Agar Gel Leishmania biology Base Sequence Virion RNA virus biochemical phenomena metabolism and nutrition biology.organism_classification Mutational analysis Open reading frame Mutagenesis Insect Science Delivery system Macromolecule Research Article |
| Zdroj: | Journal of virology. 68(12) |
| ISSN: | 0022-538X |
| Popis: | The virion of Leishmania RNA virus is predicted to be composed of a 742-amino-acid major capsid protein and a small percentage of capsid-polymerase fusion molecules. Recently, the capsid protein alone was expressed and shown to spontaneously assemble into viruslike particles. Since the major structural protein of the virion shell self-assembles into viruslike particles when expressed in the baculovirus expression system, assembly of the virion can be studied by mutational analysis and expression of a single open reading frame. In this study, several deletions and one addition of the capsid protein of Leishmania RNA virus LRV1-4 were generated. These mutants show different degrees of assembly. Assembly domains are being identified such that the capsid protein may be used as a macromolecular packaging and delivery system for Leishmania species. |
| Databáze: | OpenAIRE |
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