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Journal of Virology, August 2001, p. 7672-7682, Vol. 75, No. 16
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.16.7672-7682.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Endoplasmic Reticulum and cis-Golgi Localization of Human T-Lymphotropic Virus Type 1 p12I: Association with Calreticulin and Calnexin

Wei Ding,1 Björn Albrecht,1 Rushu Luo,2 Weiqing Zhang,1,dagger James R. L. Stanley,1 Garret C. Newbound,1,Dagger and Michael D. Lairmore1,3,4,*

Center for Retrovirus Research and Department of Veterinary Biosciences,1 Department of Neuroscience, Neurobiotechnology Center,2 Comprehensive Cancer Center, The Arthur G. James Cancer Hospital and Solove Research Institute,3 and Department of Molecular Virology, Immunology and Medical Genetics,4 The Ohio State University, Columbus, Ohio 43210

Received 12 March 2001/Accepted 18 May 2001

Human T-lymphotropic virus type 1 (HTLV-1) is a complex retrovirus encoding regulatory and accessory genes in four open reading frames (ORF I to IV) of the pX region. We have demonstrated an important role of pX ORF I expression, which encodes p12I, in establishment of HTLV-1 infection in a rabbit model and for optimal viral infectivity in quiescent primary lymphocytes. These data indicated that p12I may enhance lymphocyte activation and thereby promote virus infection. To further define the role of p12I in cell activation, we characterized the subcellular localization of p12I in transfected 293T cells and HeLa-Tat cells by multiple methods, including immunofluorescence confocal microscopy, electron microscopy, and subcellular fractionation. Herein, we demonstrate that p12I accumulates in the endoplasmic reticulum (ER) and cis-Golgi apparatus. The location of p12I was unchanged following treatments with both cycloheximide (blocking de novo protein synthesis) and brefeldin A (disrupting ER-to-Golgi protein transport), indicating that the protein is retained in the ER and cis-Golgi. Moreover, using coimmunoprecipitation assays, we identify the direct binding of p12I with both calreticulin and calnexin, resident ER proteins which regulate calcium storage. Our results indicate that p12I directly binds key regulatory proteins involved in calcium-mediated cell signaling and suggest a role of p12I in the establishment of HTLV-1 infection by activation of host cells.

* Corresponding author. Mailing address: Center for Retrovirus Research and Department of Veterinary Biosciences, The Ohio State University, 1925 Coffey Rd., Columbus, OH 43210-1092. Phone: (614) 292-4819. Fax: (614) 292-6473. E-mail: Lairmore.1{at}osu.edu.

dagger Present address: Center for Molecular Biology of Oral Diseases, College of Dentistry, University of Illinois at Chicago, Chicago, IL 60612-7213.

Dagger Present address: Elanco Animal Health, Greenfield, IN 46140.

Journal of Virology, August 2001, p. 7672-7682, Vol. 75, No. 16
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.16.7672-7682.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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