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Identification of Retroviral Late Domains as Determinants of Particle Size
- Source :
- Journal of Virology. 73:2309-2320
- Publication Year :
- 1999
- Publisher :
- American Society for Microbiology, 1999.
-
Abstract
- Retroviral Gag proteins, in the absence of any other viral products, induce budding and release of spherical, virus-like particles from the plasma membrane. Gag-produced particles, like those of authentic retrovirions, are not uniform in diameter but nevertheless fall within a fairly narrow distribution of sizes. For the human immunodeficiency virus type 1 (HIV-1) Gag protein, we recently reported that elements important for controlling particle size are contained within the C-terminal region of Gag, especially within the p6 sequence (L. Garnier, L. Ratner, B. Rovinski, S.-X. Cao, and J. W. Wills, J. Virol. 72:4667–4677, 1998). Deletions and substitutions throughout this sequence result in the release of very large particles. Because the size determinant could not be mapped to any one of the previously defined functions within p6, it seemed likely that its activity requires the overall proper folding of this region of Gag. This left open the possibility of the size determinant residing in a subdomain of p6, and in this study, we examined whether the late domain (the region of Gag that is critical for the virus-cell separation step) is involved in controlling particle size. We found that particles of normal size are produced when p6 is replaced with the totally unrelated late domain sequences from Rous sarcoma virus (contained in its p2b sequence) or equine infectious anemia virus (contained in p9). In addition, we found that the large particles released in the absence of p6 require the entire CA and adjacent spacer peptide sequences, whereas these internal sequences of HIV-1 Gag are not needed for budding (or proper size) when a late domain is present. Thus, it appears the requirements for budding are very different in the presence and absence of p6.
- Subjects :
- viruses
Immunology
Gene Products, gag
Biology
Microbiology
Virus
Viral Matrix Proteins
Equine infectious anemia
Capsid
Virology
Animals
Particle Size
Nucleocapsid
Rous sarcoma virus
Budding
Viral matrix protein
Structure and Assembly
Virion
Group-specific antigen
biology.organism_classification
Cell biology
Retroviridae
Insect Science
COS Cells
HIV-1
Particle size
Subjects
Details
- ISSN :
- 10985514 and 0022538X
- Volume :
- 73
- Database :
- OpenAIRE
- Journal :
- Journal of Virology
- Accession number :
- edsair.doi.dedup.....44d038dd78ab0ec0017a0f0848ac7ba0
- Full Text :
- https://doi.org/10.1128/jvi.73.3.2309-2320.1999