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Vaccinia virus A28L gene encodes an essential protein component of the virion membrane with intramolecular disulfide bonds formed by the viral cytoplasmic redox pathway.
- Source :
-
Journal of virology [J Virol] 2004 Mar; Vol. 78 (5), pp. 2348-56. - Publication Year :
- 2004
-
Abstract
- We report the initial characterization of the product of the vaccinia virus A28L gene, which is highly conserved in all sequenced poxviruses. Our studies showed that the A28 protein is expressed at late times during the virus replication cycle and is a membrane component of the intracellular mature virion. An N-terminal hydrophobic sequence, present in all poxvirus A28 orthologs, anchors the protein in the virion surface membrane so that most of it is exposed to the cytoplasm. The cytoplasmic domain contains four conserved cysteines, which form two intramolecular disulfide bonds. Disulfide bond formation depended on the expression of three viral proteins, E10, A2.5, and G4, which together comprise a conserved cytoplasmic redox pathway. A28 is the third identified substrate of this pathway; the others are the L1 and F9 proteins. We constructed a conditional-lethal recombinant vaccinia virus with an inducible A28L gene. The recombinant virus was propagated in the presence of inducer but was unable to replicate and spread in its absence. During a single round of an abortive infection in the absence of inducer, the synthesis and processing of viral proteins, assembly of intra- and extracellular virions, and formation of actin tails occurred normally. In another paper (T. Senkevich, B. M. Ward, and B. Moss, J. Virol. 78:2357-2366, 2004), we have demonstrated that virions assembled without A28 cannot carry out a second round of infection because they are defective in cell penetration.
- Subjects :
- Amino Acid Sequence
Animals
Cell Line
Cytoplasm ultrastructure
HeLa Cells
Humans
Molecular Sequence Data
Oxidation-Reduction
Substrate Specificity
Vaccinia virus genetics
Vaccinia virus physiology
Vaccinia virus ultrastructure
Viral Core Proteins biosynthesis
Viral Core Proteins metabolism
Viral Proteins biosynthesis
Viral Proteins chemistry
Viral Proteins genetics
Virion genetics
Virion metabolism
Virion ultrastructure
Virus Replication
Cytoplasm metabolism
Disulfides metabolism
Genes, Essential
Genes, Viral genetics
Vaccinia virus metabolism
Viral Proteins metabolism
Virion chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0022-538X
- Volume :
- 78
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Journal of virology
- Publication Type :
- Academic Journal
- Accession number :
- 14963131
- Full Text :
- https://doi.org/10.1128/jvi.78.5.2348-2356.2004