Solution Properties of Murine Leukemia Virus Gag Protein: Differences from HIV-1 Gag
| Autor: | Yun-Xing Wang, Alan Rein, Patrick K. Clark, Siddhartha A. K. Datta, Xiaobing Zuo, Stephen J. Campbell |
|---|---|
| Rok vydání: | 2011 |
| Předmět: |
Conformational change
viruses Molecular Sequence Data Immunology Gene Products gag Microbiology Mice Retrovirus Virology Scattering Small Angle Murine leukemia virus Animals Humans Amino Acid Sequence Gammaretrovirus biology Structure and Assembly C-terminus Group-specific antigen biology.organism_classification Molecular biology Protein Structure Tertiary Leukemia Virus Murine Solutions Capsid Insect Science Mutation HIV-1 Nucleic acid Biophysics |
| Zdroj: | Journal of Virology. 85:12733-12741 |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.05889-11 |
| Popis: | Immature retrovirus particles are assembled from the multidomain Gag protein. In these particles, the Gag proteins are arranged radially as elongated rods. We have previously characterized the properties of HIV-1 Gag in solution. In the absence of nucleic acid, HIV-1 Gag displays moderately weak interprotein interactions, existing in monomer-dimer equilibrium. Neutron scattering and hydrodynamic studies suggest that the protein is compact, and biochemical studies indicate that the two ends can approach close in three-dimensional space, implying the need for a significant conformational change during assembly. We now describe the properties of the Gag protein of Moloney murine leukemia virus (MLV), a gammaretrovirus. We found that this protein is very different from HIV-1 Gag: it has much weaker protein-protein interaction and is predominantly monomeric in solution. This has allowed us to study the protein by small-angle X-ray scattering and to build a low-resolution molecular envelope for the protein. We found that MLV Gag is extended in solution, with an axial ratio of ∼7, comparable to its dimensions in immature particles. Mutational analysis suggests that runs of prolines in its matrix and p12 domains and the highly charged stretch at the C terminus of its capsid domain all contribute to this extended conformation. These differences between MLV Gag and HIV-1 Gag and their implications for retroviral assembly are discussed. |
| Databáze: | OpenAIRE |
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