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Journal of Virology, March 2008, p. 2570-2574, Vol. 82, No. 5
0022-538X/08/$08.00+0     doi:10.1128/JVI.01717-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Probing the Structural States of Human Immunodeficiency Virus Type 1 Pr55gag by Using Monoclonal Antibodies{triangledown} ,{dagger}

Jason J. LeBlanc,1 Omar Perez,2 and Thomas J. Hope1*

Department of Cell and Molecular Biology, Northwestern University Feinberg School of Medicine, Chicago, Illinois 60611,1 Department of Microbiology and Immunology, University of Illinois at Chicago, Chicago, Illinois 606122

Received 7 August 2007/ Accepted 13 December 2007

Gag-FP (fluorescent protein) fusion constructs are commonly used to study human immunodeficiency virus type 1 assembly, yielding diffuse signals throughout the cytoplasm along with punctate signals routinely described as virus-like particles (VLPs) representing assembled but unprocessed Gag. However, these particles cannot be accurately described as VLPs, since fluorescence microscopy cannot provide structural resolution. We demonstrate here that the inability of a monoclonal p24 antibody to bind its cognate epitope when unprocessed Gag is assembled distinguishes VLPs from unassembled, monomeric Gag. Furthermore, we show that assembled and unassembled Gag punctate signals travel along microtubules. These monoclonal antibody studies provide a new tool for examining retroviral assembly.

* Corresponding author. Mailing address: Department of Cell and Molecular Biology, Northwestern University Feinberg School of Medicine, 303 E. Chicago Ave., Chicago, IL 60611. Phone: (312) 503-1360. Fax: (312) 503-2696. E-mail: thope{at}northwestern.edu

{triangledown} Published ahead of print on 19 December 2007.

{dagger} Supplemental material for this article may be found at http://jvi.asm.org/.

Journal of Virology, March 2008, p. 2570-2574, Vol. 82, No. 5
0022-538X/08/$08.00+0     doi:10.1128/JVI.01717-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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