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Journal of Virology, July 2003, p. 8108-8115, Vol. 77, No. 14
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.14.8108-8115.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Human Herpesvirus 7 Open Reading Frame U12 Encodes a Functional ß-Chemokine Receptor

Kazushi Nakano,1 Kenjiro Tadagaki,1 Yuji Isegawa,2 Mya Mya Aye,3 Ping Zou,4 and Koichi Yamanishi1*

Department of Microbiology C1,1 Division of Advanced Medical Bacteriology G5, Osaka University Medical School, Suita, Osaka,2 Department of Microbiology, Hyogo College of Medicine, Nishinomiya, Hyogo, Japan,4 Department of Microbiology, Institute of Medicine, Yangon, Burma3

Received 23 December 2002/ Accepted 24 April 2003

Human herpesvirus 7 (HHV-7), which belongs to the betaherpesvirus subfamily, infects mainly CD4+ T cells in vitro and infects children during infancy. After the primary infection, HHV-7 becomes latent. HHV-7 contains two genes (U12 and U51) that encode putative homologs of cellular G-protein-coupled receptors. To analyze the biological function of the U12 gene, we cloned the gene and expressed the U12 protein in cells. The U12 gene encoded a calcium-mobilizing receptor for the EBI1 ligand chemokine-macrophage inflammatory protein 3ß (ELC/MIP-3ß) but not for other chemokines, suggesting that the chemokine selectivity of the U12 gene product is distinct from that of the known mammalian chemokine receptors. These studies revealed that U12 activates distinct transmembrane signaling pathways that may mediate biological functions by binding with a ß-chemokine, ELC/MIP-3ß.

* Corresponding author. Mailing address: Department of Microbiology C1, Osaka University Medical School, 2-2 Yamada-oka, Suita, Osaka 565-0871, Japan. Phone: 81-6-6879-3323. Fax: 81-6-6879-3329. E-mail: yamanisi{at}micro.med.osaka-u.ac.jp.

Journal of Virology, July 2003, p. 8108-8115, Vol. 77, No. 14
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.14.8108-8115.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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