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Journal of Virology, January 2004, p. 595-602, Vol. 78, No. 2
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.2.595-602.2004

Identification of an Extracellular Domain within the Human PiT2 Receptor That Is Required for Amphotropic Murine Leukemia Virus Binding

Steven A Feldman, Karen B. Farrell, Ravi K. Murthy, Jill L. Russ, and Maribeth V. Eiden*

Section on Molecular Virology, Laboratory of Cellular and Molecular Regulation, National Institute of Mental Health, Bethesda, Maryland 20892

Received 10 July 2003/ Accepted 3 October 2003

Human PiT2 (PiT2) is a multiple-membrane-spanning protein that functions as a type III sodium phosphate cotransporter and as the receptor for amphotropic murine leukemia virus (A-MuLV). Human PiT1 (PiT1), another type III sodium phosphate cotransporter, is a highly related protein that functions as a receptor for gibbon ape leukemia virus but not for A-MuLV. The ability of PiT1 and PiT2 to function as discrete viral receptors with unique properties presumably is reflected in critical residue differences between these two proteins. Early efforts to map the region(s) within PiT2 that is important for virus binding and/or entry relied on infection results obtained with PiT1-PiT2 chimeric cDNAs expressed in Chinese hamster ovary (CHOK1) cells. These attempts to localize the PiT2 virus-binding site were hampered because they were based on infectivity, not binding, assays, and therefore, receptors that bound but failed to facilitate virus entry could not be distinguished from receptors that did not bind virus. Using a more accurate topological model for PiT2 as well as an A-MuLV receptor-binding assay, we have identified extracellular domain one (ECD1) of the human PiT2 receptor as being important for A-MuLV binding and infection.

* Corresponding author. Mailing address: Laboratory of Cellular and Molecular Regulation, NIMH, Building 36, Rm. 2A11, 9000 Rockville Pike, Bethesda, MD 20892-4068. Phone: (301) 402-1641. Fax: (301) 402-5358. E-mail: eidenm{at}mail.nih.gov.

Journal of Virology, January 2004, p. 595-602, Vol. 78, No. 2
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.2.595-602.2004




This article has been cited by other articles:

  • Farrell, K. B., Tusnady, G. E., Eiden, M. V. (2009). New Structural Arrangement of the Extracellular Regions of the Phosphate Transporter SLC20A1, the Receptor for Gibbon Ape Leukemia Virus. J. Biol. Chem. 284: 29979-29987 [Abstract] [Full Text]  
  • Manel, N., Battini, J.-L., Sitbon, M. (2005). Human T Cell Leukemia Virus Envelope Binding and Virus Entry Are Mediated by Distinct Domains of the Glucose Transporter GLUT1. J. Biol. Chem. 280: 29025-29029 [Abstract] [Full Text]  
  • Farrell, K. B., Eiden, M. V. (2005). Dissection of Gammaretroviral Receptor Function by Using Type III Phosphate Transporters as Models. J. Virol. 79: 9332-9336 [Abstract] [Full Text]  
  • Bottger, P., Pedersen, L. (2004). The Central Half of Pit2 Is Not Required for Its Function as a Retroviral Receptor. J. Virol. 78: 9564-9567 [Abstract] [Full Text]  


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