Matrix protein of Akv murine leukemia virus: genetic mapping of regions essential for particle formation
| Autor: | Finn Skou Pedersen, E C Jørgensen, Poul Jørgensen |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1992 |
| Předmět: |
DNA Replication
Genes Viral Transcription Genetic viruses Immunology Molecular Sequence Data Gene Products gag Sequence alignment Biology medicine.disease_cause Microbiology Myristic Acid Viral Matrix Proteins Proviruses Virology Murine leukemia virus Virus maturation medicine Amino Acid Sequence Cloning Molecular Peptide sequence chemistry.chemical_classification Mutation Viral matrix protein Base Sequence Genetic Complementation Test Chromosome Mapping Group-specific antigen biology.organism_classification Molecular biology Amino acid Leukemia Virus Murine Kinetics chemistry Insect Science DNA Viral Myristic Acids Sequence Alignment Research Article |
| Zdroj: | Bonefeld-Jørgensen, E C, Pedersen, F S & Jørgensen, P 1992, ' Matrix protein of Akv murine leukemia virus: genetic mapping of regions essential for particle formation ', Journal of Virology, vol. 66, no. 7, pp. 4479-87 . |
| Popis: | Udgivelsesdato: 1992-Jul Type C retroviruses assemble at the plasma membrane of the infected cell. Attachment of myristic acid to the N terminus of the Gag precursor polyprotein has been shown to be essential for membrane localization and virus morphogenesis. Here, we report that the matrix (MA) protein contains regions that in conjunction with myristylation are important for Gag protein stability and the assembly of murine leukemia viruses. We identified these domains by generating a series of Akv murine leukemia virus mutants carrying small in-frame deletions within the coding region of the MA protein encompassing 129 amino acids. Studies show that mutants with deletions within the segment encoding the first 102 amino acids were all replication defective, whereas the C-terminal residues 103 to 124 seem not to have any critical function in virus maturation. Cells expressing the replication-defective genomes did not release any detectable Gag proteins. In one mutant, deletion of 3 amino acids in the N terminus resulted in an inefficiently myristylated, stable Gag polyprotein. The remaining defect genomes encoded unstable Gag proteins, although they were modified with myristic acid. The results suggest that the matrix domain plays an important role in stabilizing the Gag polyprotein. |
| Databáze: | OpenAIRE |
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