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Journal of Virology, February 2006, p. 1619-1628, Vol. 80, No. 4
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.4.1619-1628.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Envelope Determinants for Dual-Receptor Specificity in Feline Leukemia Virus Subgroup A and T Variants

Heather H. Cheng,1,3 Maria M. Anderson,3 F. Claire Hankenson,2,3,{dagger} Lily Johnston,3 Chitra V. Kotwaliwale,1,3 and Julie Overbaugh3*

Program in Molecular and Cellular Biology,1 Department of Microbiology, University of Washington,2 Division of Human Biology, Fred Hutchinson Cancer Research Center, Seattle, Washington3

Received 18 February 2005/ Accepted 18 November 2005

Gammaretroviruses, including the subgroups A, B, and C of feline leukemia virus (FeLV), use a multiple-membrane-spanning transport protein as a receptor. In some cases, such as FeLV-T, a nonclassical receptor that includes both a transport protein (Pit1) and a soluble cofactor (FeLIX) is required for entry. To define which regions confer specificity to classical versus nonclassical receptor pathways, we engineered mutations found in either FeLV-A/T or FeLV-T, individually and in combination, into the backbone of the transmissible form of the virus, FeLV-A. The receptor specificities of these viruses were tested by measuring infection and binding to cells expressing the FeLV-A receptor or the FeLV-T receptors. FeLV-A receptor specificity was maintained when changes at amino acid position 6, 7, or 8 of the mature envelope glycoprotein were introduced, although differences in infection efficiency were observed. When these N-terminal mutations were introduced together with a C-terminal 4-amino-acid insertion and an adjacent amino acid change, the resulting viruses acquired FeLV-T receptor specificity. Additionally, a W->L change at amino acid position 378, although not required, enhanced infectivity for some viruses. Thus, we have found that determinants in the N and C termini of the envelope surface unit can direct entry via the nonclassical FeLV-T receptor pathway. The region that has been defined as the receptor binding domain of gammaretroviral envelope proteins determined entry via the FeLV-A receptor independently of the presence of the N- and C-terminal FeLV-T receptor determinants.

* Corresponding author. Mailing address: Division of Human Biology, Fred Hutchinson Cancer Research Center, 1100 Fairview Ave. N., Mail Stop C3-168, Seattle, WA 98109-1024. Phone: (206) 667-3524. Fax: (206) 667-1535. E-mail: joverbau{at}fhcrc.org.

{dagger} Present address: Unit for Laboratory Animal Medicine, University of Michigan, Ann Arbor, MI 48109.

Journal of Virology, February 2006, p. 1619-1628, Vol. 80, No. 4
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.4.1619-1628.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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