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The conformation of the mature dimeric human immunodeficiency virus type 1 RNA genome requires packaging of pol protein

Shehu-Xhilaga, M., Hill, M., Marshall, J. A., Kappes, J., Crowe, S. M. and Mak, J. 2002, The conformation of the mature dimeric human immunodeficiency virus type 1 RNA genome requires packaging of pol protein, Journal of virology, vol. 76, no. 9, pp. 4331-4340, doi: 10.1128/JVI.76.9.4331-4340.2002.

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Title The conformation of the mature dimeric human immunodeficiency virus type 1 RNA genome requires packaging of pol protein
Author(s) Shehu-Xhilaga, M.
Hill, M.
Marshall, J. A.
Kappes, J.
Crowe, S. M.
Mak, J.ORCID iD for Mak, J. orcid.org/0000-0002-5229-5707
Journal name Journal of virology
Volume number 76
Issue number 9
Start page 4331
End page 4340
Total pages 10
Publisher American Society for Microbiology
Place of publication Washington, D. C.
Publication date 2002-05
ISSN 0022-538X
1098-5514
Keyword(s) gag protein
integrase
Pol protein
protein precursor
RNA directed DNA polymerase
virus RNA
Summary The packaging of a mature dimeric RNA genome is an essential step in human immunodeficiency virus type 1 (HIV-1) replication. We have previously shown that overexpression of a protease (PR)-inactive HIV-1 Gag-Pro-Pol precursor protein generates noninfectious virions that contain mainly monomeric RNA (M. Shehu-Xhilaga, S. M. Crowe, and J. Mak, J. Virol. 75:1834-1841, 2001). To further define the contribution of HIV-1 Gag and Gag-Pro-Pol to RNA maturation, we analyzed virion RNA dimers derived from Gag particles in the absence of Gag-Pro-Pol. Compared to wild-type (WT) dimeric RNAs, these RNA dimers have altered mobility and low stability under electrophoresis conditions, suggesting that the HIV-1 Gag precursor protein alone is not sufficient to stabilize the dimeric virion RNA structure. The inclusion of an active viral PR, without reverse transcriptase (RT) and integrase (IN), rescued the stability of the virion RNA dimers in the Gag particles but did not restore the mobility of the RNAs, suggesting that RT and IN are also required for virion RNA dimer maturation. Thin-section electron microscopy showed that viral particles deficient in RT and IN contain empty cone-shaped cores. The abnormal core structure indicates a requirement for Gag-Pro-Pol packaging during core maturation. Supplementing viral particles with either RT or IN via Vpr-RT or Vpr-IN alone did not correct the conformation of the dimer RNAs, whereas expression of both RT and IN in trans as a Vpr-RT-IN fusion restored RNA dimer conformation to that of the WT virus and also restored the electron-dense, cone-shaped virion core characteristic of WT virus. Our data suggest a role for RT-IN in RNA dimer conformation and the formation of the electron-dense viral core.
Language eng
DOI 10.1128/JVI.76.9.4331-4340.2002
Field of Research 119999 Medical and Health Sciences not elsewhere classified
Socio Economic Objective 970111 Expanding Knowledge in the Medical and Health Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
Copyright notice ©2002, American Society for Microbiology
Persistent URL http://hdl.handle.net/10536/DRO/DU:30047534

Document type: Journal Article
Collections: School of Medicine
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Every reasonable effort has been made to ensure that permission has been obtained for items included in DRO. If you believe that your rights have been infringed by this repository, please contact drosupport@deakin.edu.au.