The Assembly Domain of the Small Capsid Protein of Kaposi's Sarcoma-Associated Herpesvirus
| Autor: | C. M. Capuano, J. M. McCaffery, Daniel C. Anacker, Brandon Henson, Erin N. Pryce, Prashant Desai, Dale F. Kreitler |
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| Rok vydání: | 2012 |
| Předmět: |
viruses
Genetic Vectors Molecular Sequence Data Immunology Biology medicine.disease_cause Microbiology Cell Line law.invention Domain (software engineering) Viral Proteins law Virology medicine Animals Protein Interaction Domains and Motifs Amino Acid Sequence Kaposi's sarcoma-associated herpesvirus Alanine Insect cell Virus Assembly Structure and Assembly Virion Microscopy Electron Amino Acid Substitution Capsid Insect Science Herpesvirus 8 Human Mutagenesis Site-Directed Recombinant DNA Mutant Proteins Baculoviridae Sequence Alignment |
| Zdroj: | Journal of Virology. 86:11926-11930 |
| ISSN: | 1098-5514 0022-538X |
| DOI: | 10.1128/jvi.01430-12 |
| Popis: | Self-assembly of Kaposi's sarcoma-associated herpesvirus capsids occurs when six proteins are coexpressed in insect cells using recombinant baculoviruses; however, if the small capsid protein (SCP) is omitted from the coinfection, assembly does not occur. Herein we delineate and identify precisely the assembly domain and the residues of SCP required for assembly. Hence, six residues, R14, D18, V25, R46, G66, and R70 in the assembly domain, when changed to alanine, completely abolish or reduce capsid assembly. |
| Databáze: | OpenAIRE |
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