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© The Rockefeller University Press, 0022-1007/1997/6/2015/ $5.00
The Journal of Experimental Medicine, Volume 185, Number 11, June 2, 1997 2015-2023

Article

STRL33, A Novel Chemokine Receptor–like Protein, Functions as a Fusion Cofactor for Both Macrophage-tropic and T Cell Line–tropic HIV-1

Fang Liao*, Ghalib Alkhatib{ddagger}, Keith W.C. Peden§, Geetika Sharma*, Edward A. Berger{ddagger}, and Joshua M. Farber*

From the * Laboratory of Clinical Investigation; {ddagger} Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland; and the § Laboratory of Retrovirus Research, Center for Biologics, Evaluation and Research, Food and Drug Administration, Bethesda, Maryland 20892

The chemokine receptors CXCR4, CCR2B, CCR3, and CCR5 have recently been shown to serve along with CD4 as coreceptors for HIV-1. The tropisms of HIV-1 strains for subgroups of CD4+ cells can be explained, at least partly, by the selective use of G protein–coupled receptors (GPCRs). We have identified a novel human gene, STRL33, located on chromosome 3 that encodes a GPCR with sequence similarity to chemokine receptors and to chemokine receptor–like orphan receptors. STRL33 is expressed in lymphoid tissues and activated T cells, and is induced in activated peripheral blood lymphocytes. When transfected into nonhuman NIH 3T3 cells expressing human CD4, the STRL33 cDNA rendered these cells competent to fuse with cells expressing HIV-1 envelope glycoproteins (Envs). Of greatest interest, STRL33, in contrast with CXCR4 or CCR5, was able to function as a cofactor for fusion mediated by Envs from both T cell line–tropic and macrophage-tropic HIV-1 strains. STRL33-transfected Jurkat cell lines also supported enhanced productive infection with HIV-1 compared with control Jurkat cells. Despite the sequence similarities between STRL33 and chemokine receptors, STRL33-transfected cell lines did not respond to any in a panel of chemokines. Based on the pattern of tissue expression of the STRL33 mRNA, and given the ability of STRL33 to function with Envs of differing tropisms, STRL33 may play a role in the establishment and/or progression of HIV-1 infection.

Address correspondence to Joshua M. Farber, Building 10, Room 11N-228, National Institutes of Health, 9000 Rockville Pike, Bethesda, Maryland 20892.

Thanks are due to J. Yannelli, P. Murphy, S. Ahuja, C. Combadière, Y. Chang, R. Siliciano, and M. Tsang for reagents and/or helpful discussions.

1Abbreviations used in this paper: β-Gal, β-galactosidase; Envs, envelope glycoproteins; FBS, fetal bovine serum; GPCRs, G protein–coupled receptors; HEK, human embryonic kidney; M-tropic, macrophage tropic; ORF, open reading frame; TCL-tropic, T cell line tropic; TIL, tumorinfiltrating lymphocytes; TMD, transmembrane domain.


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