Conserved serines in simian immunodeficiency virus capsid are required for virus budding
Autor: | Janice E. Clements, Sarah M. Rue, Jason W. Roos, Sheila A. Barber |
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Rok vydání: | 2004 |
Předmět: |
viruses
Molecular Sequence Data Biology medicine.disease_cause Virus Replication Phosphoamino acid analysis Virus 03 medical and health sciences Capsid 0302 clinical medicine Genes Reporter Virology medicine Serine Amino Acid Sequence Viral shedding Phosphorylation Luciferases Conserved Sequence 030304 developmental biology Gag 0303 health sciences Budding RNA-Directed DNA Polymerase Simian immunodeficiency virus Molecular biology 3. Good health SIV Viral replication Amino Acid Substitution Mutagenesis Site-Directed Capsid Proteins Simian Immunodeficiency Virus 030215 immunology |
Zdroj: | Virology. 336(1) |
ISSN: | 0042-6822 |
Popis: | The simian immunodeficiency virus (SIV) capsid protein (CA), a constituent of the Pr55 Gag polyprotein, is phosphorylated in virions but not in virus-producing cells (Rue, S.M., Roos, J.W., Tarwater, P.M., Clements, J.E., Barber, S.A., 2005. Phosphorylation and proteolytic cleavage of gag proteins in budded simian immunodeficiency virus. J. Virol. 79 (4), 2484–2492.). Using phosphoamino acid analysis of CA, we show that serine is the primary phosphate acceptor. A series of substitution mutants of serines in the CA domain of Pr55 Gag were constructed in the infectious viral clone SIVmac239. These virus mutants were examined for defects in virus replication and virion infectivity, release, and morphology, as well as alterations in phosphorylation of CA-containing proteins. Although the virus mutants exhibited a number of replication defects, none of these defects could be directly attributed to aberrant CA phosphorylation. A novel defect was a block in early budding, which was common among several virus mutants with substitutions in the CA N terminus. Together, these results indicate that certain residues in the CA N terminus are crucial for early budding events. |
Databáze: | OpenAIRE |
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