Functional domains of the capsid protein of human immunodeficiency virus type 1
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- T Dorfman
- Division of Human Retrovirology, Dana-Farber Cancer Institute, Boston, Massachusetts 02115.
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- A Bukovsky
- Division of Human Retrovirology, Dana-Farber Cancer Institute, Boston, Massachusetts 02115.
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- A Ohagen
- Division of Human Retrovirology, Dana-Farber Cancer Institute, Boston, Massachusetts 02115.
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- S Höglund
- Division of Human Retrovirology, Dana-Farber Cancer Institute, Boston, Massachusetts 02115.
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- H G Göttlinger
- Division of Human Retrovirology, Dana-Farber Cancer Institute, Boston, Massachusetts 02115.
書誌事項
- 公開日
- 1994-12
- 権利情報
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- https://journals.asm.org/non-commercial-tdm-license
- DOI
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- 10.1128/jvi.68.12.8180-8187.1994
- 公開者
- American Society for Microbiology
この論文をさがす
説明
<jats:p>A series of deletions was introduced into the CA domain of the human immunodeficiency virus type 1 Gag polyprotein to examine its role in virus particle and core formation. The mutations resulted in two phenotypes, indicating the existence of two functionally distinct regions within the CA domain. Deletions within a conserved stretch of 20 amino acids referred to as the major homology region (MHR) and deletions C terminal to this region blocked virus replication and significantly reduced the ability to form viral particles. Deletions N terminal to the MHR also prevented virus replication, but the mutants retained the ability to assemble and release viral particles with the same efficiency as the wild-type virus. The mutant particles contained circular rather than cone-shaped cores, and while they were of a density similar to that of wild-type particles, they were more heterogeneous in size. These results indicate that CA domain sequences N terminal to the MHR are essential for the morphogenesis of the mature cone-shaped core.</jats:p>
収録刊行物
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- Journal of Virology
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Journal of Virology 68 (12), 8180-8187, 1994-12
American Society for Microbiology