JVI Figure table search 04
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Clever, J. L.
Right arrow Articles by Parslow, T. G.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Clever, J. L.
Right arrow Articles by Parslow, T. G.

 Previous Article  |  Next Article 

Journal of Virology, January 2000, p. 541-546, Vol. 74, No. 1
0022-538X/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

A Heterologous, High-Affinity RNA Ligand for Human Immunodeficiency Virus Gag Protein Has RNA Packaging Activity

Jared L. Clever,1,2,dagger Randy A. Taplitz,3,Dagger Michael A. Lochrie,4 Barry Polisky,4,§ and Tristram G. Parslow1,2,*

Departments of Pathology,1 Microbiology and Immunology,2 and Internal Medicine,3 University of California, San Francisco, California 94143-0506, and NeXstar Pharmaceuticals, Inc., Boulder, Colorado 803014

Received 22 July 1999/Accepted 28 September 1999

Retroviral RNA encapsidation depends on the specific binding of Gag proteins to packaging (psi ) signals in genomic RNA. We investigated whether an in vitro-selected, high-affinity RNA ligand for the nucleocapsid (NC) portion of the Gag protein from human immunodeficiency virus type 1 (HIV-1) could mediate packaging into HIV-1 virions. We find that this ligand can functionally substitute for one of the Gag-binding elements (termed SL3) in the HIV-1 psi  locus to support packaging and viral infectivity in cis. By contrast, this ligand, which fails to dimerize spontaneously in vitro, is unable to replace a different psi  element (termed SL1) which is required for both Gag binding and dimerization of the HIV-1 genome. A single point mutation within the ligand that eliminates high-affinity in vitro Gag binding also abolishes its packaging activity at the SL3 position. These results demonstrate that specific binding of Gag or NC protein is a critical determinant of genomic RNA packaging.

* Corresponding author. Mailing address: Department of Pathology, Box 0506, University of California, San Francisco, CA 94143-0506. Phone: (415) 476-1015. Fax: (415) 476-9672. E-mail: parslow{at}cgl.ucsf.edu.

dagger Present address: Department of Microbiology, University of Texas Health Sciences Center at San Antonio, San Antonio, TX 78284-7758.

Dagger Present address: Department of Medicine, Oregon Health Sciences University, Portland, OR 97201.

§ Present address: BioStar, Inc., Boulder, CO 80301.

Journal of Virology, January 2000, p. 541-546, Vol. 74, No. 1
0022-538X/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:



Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. Mol. Cell. Biol. Microbiol. Mol. Biol. Rev.
Clin. Vaccine Immunol. ALL ASM JOURNALS

Copyright © 2000 by the American Society for Microbiology. All rights reserved.