This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Dreyer, K.
Right arrow Articles by Pedersen, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Dreyer, K.
Right arrow Articles by Pedersen, L.

 Previous Article  |  Next Article 

Journal of Virology, March 2000, p. 2926-2929, Vol. 74, No. 6
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

A 13-Amino-Acid Pit1-Specific Loop 4 Sequence Confers Feline Leukemia Virus Subgroup B Receptor Function upon Pit2

Kasper Dreyer,1 Finn S. Pedersen,1,2 and Lene Pedersen1,*

Department of Molecular and Structural Biology1 and Department of Medical Microbiology and Immunology,2 University of Aarhus, DK-8000 Aarhus C, Denmark

Received 23 July 1999/Accepted 8 December 1999

Feline leukemia virus subgroup B (FeLV-B) and gibbon ape leukemia virus (GALV) utilize the human protein Pit1 but not the related protein, Pit2, as receptor. A stretch of 9 amino acids, named region A, was identified in the putative fourth extracellular loop of Pit1 (residues 550 through 558) as critical for FeLV-B and GALV receptor function. However, the presence of Pit1 region A did not confer receptor function for FeLV-B upon Pit2, while it did so for GALV. We have here shown that the presence of two Pit1-specific loop 4 residues (tyrosine 546 and valine 548) in addition to Pit1 region A is sufficient to make Pit2 an efficient FeLV-B receptor; that is, a stretch of 13 amino acids encompassing all loop 4 amino acid differences between Pit1 and Pit2 comprises a C-terminal determinant for FeLV-B receptor function. Thus, the same limited receptor region is sufficient to confer receptor function for both viruses upon Pit2.

* Corresponding author. Mailing address: Department of Molecular and Structural Biology, University of Aarhus, C. F. Møllers Allé, Bldg. 130, DK-8000 Aarhus C, Denmark. Phone: 45 8942 2633. Fax: 45 8619 6500. E-mail: LP{at}mbio.aau.dk.

Journal of Virology, March 2000, p. 2926-2929, Vol. 74, No. 6
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Beck, L., Leroy, C., Salaun, C., Margall-Ducos, G., Desdouets, C., Friedlander, G. (2009). Identification of a Novel Function of PiT1 Critical for Cell Proliferation and Independent of Its Phosphate Transport Activity. J. Biol. Chem. 284: 31363-31374 [Abstract] [Full Text]  
  • Virkki, L. V., Biber, J., Murer, H., Forster, I. C. (2007). Phosphate transporters: a tale of two solute carrier families. Am. J. Physiol. Renal Physiol. 293: F643-F654 [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]  
  • Bottger, P., Pedersen, L. (2002). Two Highly Conserved Glutamate Residues Critical for Type III Sodium-dependent Phosphate Transport Revealed by Uncoupling Transport Function from Retroviral Receptor Function. J. Biol. Chem. 277: 42741-42747 [Abstract] [Full Text]  
  • Lauring, A. S., Cheng, H. H., Eiden, M. V., Overbaugh, J. (2002). Genetic and Biochemical Analyses of Receptor and Cofactor Determinants for T-Cell-Tropic Feline Leukemia Virus Infection. J. Virol. 76: 8069-8078 [Abstract] [Full Text]  
  • Salaün, C., Rodrigues, P., Heard, J. M. (2001). Transmembrane Topology of PiT-2, a Phosphate Transporter-Retrovirus Receptor. J. Virol. 75: 5584-5592 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»