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Journal of Virology, December 2000, p. 11972-11976, Vol. 74, No. 24
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Apelin, the Natural Ligand of the Orphan Seven-Transmembrane Receptor APJ, Inhibits Human Immunodeficiency Virus Type 1 Entry

Mark Cayabyab,1,2 Shuji Hinuma,3 Michael Farzan,1 Hyeryun Choe,1,4 Shoji Fukusumi,3 Chieko Kitada,3 Naoki Nishizawa,3 Masaki Hosoya,3 Osamu Nishimura,3 Tsehaynesh Messele,5 Georgios Pollakis,6 Jaap Goudsmit,6 Masahiko Fujino,3 and Joseph Sodroski1,2,*

Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Harvard Medical School,1 Department of Immunology and Infectious Diseases, Harvard School of Public Health,2 and Perlmutter Laboratory, Children's Hospital, and Department of Medicine and Pediatrics, Beth Israel Hospital and Harvard Medical School,4 Boston, Massachusetts 02115; Pharmaceutical Discovery Research Division, Takeda Chemical Industries, Ltd., Tsukuba, Ibaraki 300-4293, Japan3; Ethiopian Health and Nutrition Research Institute, Addis Ababa, Ethiopia5; and Department of Human Retrovirology, Faculty of Medicine-Academic Medical Centre, University of Amsterdam, Amsterdam, The Netherlands6

Received 6 April 2000/Accepted 22 August 2000

In addition to the CCR5 and CXCR4 chemokine receptors, a subset of primary human immunodeficiency virus type 1 (HIV-1) isolates can also use the seven-transmembrane-domain receptor APJ as a coreceptor. A previously identified ligand of APJ, apelin, specifically inhibited the entry of primary T-tropic and dualtropic HIV-1 isolates from different clades into cells expressing CD4 and APJ. Analysis of apelin analogues demonstrated that potent and specific antiviral activity was retained by a 13-residue, arginine-rich peptide. Antiviral potency was influenced by the integrity of methionine 75, which contributes to APJ-binding affinity, and by the retention of apelin residues 63 to 65. These studies demonstrate the ability of a small peptide ligand to block the function of APJ as an HIV-1 coreceptor, identify apelin sequences important for the inhibition, and provide new reagents for the investigation of the significance of APJ to HIV-1 infection and pathogenesis.

* Corresponding author. Mailing address: Dana-Farber Cancer Institute, 44 Binney St.-JFB 824, Boston, MA 02115. Phone: (617) 632-3371. Fax: (617) 632-4338. E-mail: joseph_sodroski{at}dfci.harvard.edu.

Journal of Virology, December 2000, p. 11972-11976, Vol. 74, No. 24
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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