A Val-25-to-Ile substitution in the envelope precursor polyprotein, gPr80env, is responsible for the temperature sensitivity, inefficient processing of gPr80env, and neurovirulence of ts1, a mutant of Moloney murine leukemia virus TB
| Autor: | Paul K.Y. Wong, P. F. Szurek, J. K. Ball, P. H. Yuen |
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| Rok vydání: | 1990 |
| Předmět: |
Genes
Viral medicine.medical_treatment Restriction Mapping Immunology Mutant Gene Expression Mice Inbred Strains Transfection Microbiology Endoglycosidase Cell Line Mice symbols.namesake Species Specificity Viral Envelope Proteins Viral envelope Virology Moloney Murine Leukemia Virus TB Murine leukemia virus medicine Animals Isoleucine Protein Precursors Cells Cultured Protease Virulence biology Endoplasmic reticulum Temperature Nucleic Acid Hybridization Valine Golgi apparatus biology.organism_classification Molecular biology Insect Science Mutation symbols biology.protein Moloney murine leukemia virus Protein Processing Post-Translational Research Article |
| Zdroj: | Journal of Virology. 64:467-475 |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.64.2.467-475.1990 |
| Popis: | ts1 is a neurovirulent spontaneous temperature-sensitive mutant of Moloney murine leukemia virus TB which causes hindlimb paralysis in mice. Previously, it had been shown that the temperature-sensitive defect resided in the env gene. At the restrictive temperature, the envelope precursor polyprotein, gPr80env, is inefficiently processed intracellularly into two cleavage products, gp70 and Prp15E. This inefficient processing of gPr80env is correlated with neurovirulence. In this study, it was shown that a single amino acid substitution, Val-25----Ile in gPr80env, is responsible for the temperature sensitivity, inefficient processing of gPr80env at the restrictive temperature, and neurovirulence of ts1. At the restrictive temperature, a steady-state level of nonprocessed, endoglycosidase H-sensitive gPr80env remained in the endoplasmic reticulum of cells infected by ts1, but no endoglycosidase H-resistant gPr80env and only trace amounts of gp70 were detected in the infected cells. Since the host cell-encoded processing protease resides in the cis cisternae of the Golgi apparatus, inefficient processing of gPr80env at the restrictive temperature is most likely due to inefficient transport of gPr80env from the endoplasmic reticulum to the cis cisternae of the Golgi apparatus rather than due to misfolded gPr80env being a poor substrate for the processing protease at the restrictive temperature. |
| Databáze: | OpenAIRE |
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