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Journal of Virology, January 2004, p. 1042-1049, Vol. 78, No. 2
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.2.1042-1049.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Incorporation of Pol into Human Immunodeficiency Virus Type 1 Gag Virus-Like Particles Occurs Independently of the Upstream Gag Domain in Gag-Pol

Shan Cen,1 Meijuan Niu,1 Jenan Saadatmand,1,2 Fei Guo,1 Yue Huang,3 Gary J. Nabel,3 and Lawrence Kleiman1,2,4*

Lady Davis Institute for Medical Research and McGill AIDS Centre, Jewish General Hospital,1 Departments of Medicine,2 Microbiology and Immunology, McGill University, Montreal, Quebec, Canada H3T 1E2,4 Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland3

Received 17 April 2003/ Accepted 3 October 2003

By using particle-associated reverse transcriptase (RT) activity as an assay for Pol incorporation into human immunodeficiency virus type 1 (HIV-1) Gag virus-like particles (VLPs), it has been found that truncated, protease-negative, Gag-Pol missing cis Gag sequences is still incorporated into Gag VLPs, albeit at significantly reduced levels (10 to 20% of the level of wild-type Gag-Pol). In this work, we have directly measured the incorporation of truncated Gag-Pol species into Gag VLPs and have found that truncated Gag-Pol that is missing all sequences upstream of RT is still incorporated into Gag VLPs at levels approximating 70% of that achieved by wild-type Gag-Pol. Neither protease nor integrase regions in Pol are required for its incorporation, implying an interaction between Gag and RT sequences in the Pol protein. While the incorporation of Gag-Pol into Gag VLPs is reduced 12-fold by the replacement of the nucleocapsid within Gag with a leucine zipper motif, this mutation does not affect Pol incorporation. However, the deletion of p6 in Gag reduces Pol incorporation into Gag VLPs four- to fivefold. Pol shows the same ability as Gag-Pol to selectively package tRNALys into Gag VLPs, and primer tRNA3Lys is found annealed to the viral genomic RNA. These data suggest that after the initial separation of Gag from Pol during cleavage of Gag-Pol by viral protease, the Pol species still retains the capacity to bind to both Gag and tRNA3Lys, which may be required for Pol and tRNA3Lys to be retained in the assembling virion until budding is completed.

* Corresponding author. Mailing address: Lady Davis Institute for Medical Research-Jewish General Hospital, 3755 Côte Ste-Catherine Rd., Montreal, Quebec, Canada H3T 1E2. Phone: (514) 340-8260. Fax: (514) 340-7502. E-mail: lawrence.kleiman{at}mcgill.ca.

Journal of Virology, January 2004, p. 1042-1049, Vol. 78, No. 2
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.2.1042-1049.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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  • Liao, W.-H., Huang, K.-J., Chang, Y.-F., Wang, S.-M., Tseng, Y.-T., Chiang, C.-C., Wang, J.-J., Wang, C.-T. (2007). Incorporation of Human Immunodeficiency Virus Type 1 Reverse Transcriptase into Virus-Like Particles. J. Virol. 81: 5155-5165 [Abstract] [Full Text]  
  • Girnary, R., King, L., Robinson, L., Elston, R., Brierley, I. (2007). Structure-function analysis of the ribosomal frameshifting signal of two human immunodeficiency virus type 1 isolates with increased resistance to viral protease inhibitors. J. Gen. Virol. 88: 226-235 [Abstract] [Full Text]  
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