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Journal of Virology, May 2002, p. 4267-4274, Vol. 76, No. 9
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.9.4267-4274.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Fusion-Defective Gibbon Ape Leukemia Virus Vectors Can Be Rescued by Homologous but Not Heterologous Soluble Envelope Proteins

Karen B. Farrell, Yuan-Tsang Ting, and Maribeth V. Eiden*

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

Received 19 September 2001/ Accepted 17 January 2002

Murine leukemia virus (MLV)-derived envelope proteins containing alterations in or adjacent to the highly conserved PHQ motif present at the N terminus of the envelope surface subunit (SU) are incorporated into vector particles but are not infectious due to a postbinding block to viral entry. These mutants can be rendered infectious by the addition of soluble receptor-binding domain (RBD) proteins in the culture medium. The RBD proteins that rescue the infectivity of these defective MLV vectors can be derived from the same MLV or from other MLVs that use distinct receptors to mediate entry. We have now constructed functional immunologically reactive gibbon ape leukemia virus (GALV) envelope proteins, tagged with a feline leukemia virus (FeLV)-derived epitope tag, which are efficiently incorporated into infectious particles. Tagged GALV envelope proteins bind specifically to cells expressing the phosphate transporter protein Pit1, demonstrating for the first time that Pit1 is the binding receptor for GALV and not a coreceptor or another type of GALV entry factor. We have also determined that GALV particles bearing SU proteins with an insertion C-terminal to the PHQ motif (GALV I10) bind Pit1 but fail to infect cells. Incubation with soluble GALV RBD renders GALV I10 particles infectious, whereas incubation with soluble RBDs from MLV or FeLV-B does not. This finding is consistent with the results obtained by Lauring et al. using FeLV-T, a virus that employs Pit1 as a receptor but requires soluble FeLV RBD for entry. MLV and GALV RBDs are not able to render FeLV-T infectious (A. S. Lauring, M. M. Anderson, and J. Overbaugh, J. Virol. 75:8888-8898, 2001). Together, these results suggest that fusion-defective FeLV-T and GALV are restricted to homologous RBD rescue of infectivity.

* Corresponding author. Mailing address: Building 36, Room 2A11, Unit on Molecular Virology, Laboratory of Cellular and Molecular Regulation, National Institute of Mental Health, 36 Convent Dr., MSC 4068, Bethesda, MD 20892. Phone: (301) 402-1641. Fax: (301) 402-5358. E-mail: m_eiden{at}codon.nih.gov.

Journal of Virology, May 2002, p. 4267-4274, Vol. 76, No. 9
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.9.4267-4274.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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