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Journal of Virology, May 2003, p. 5926-5932, Vol. 77, No. 10
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.10.5926-5932.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Sodium-Dependent myo-Inositol Transporter 1 Is a Cellular Receptor for Mus cervicolor M813 Murine Leukemia Virus

Sibyll Hein,1 Vladimir Prassolov,2 Yuanming Zhang,3 Dmitry Ivanov,2 Jürgen Löhler,4 Susan R. Ross,3 and Carol Stocking1*

Department of Cell and Virus Genetics,1 Molecular Pathology Group, Heinrich-Pette-Institute for Experimental ImmunologyVirology, D-20251 Hamburg, Germany,4 Engelhardt Institute of Molecular Biology, Moscow, Russia 119991,2 Department of Microbiology and Cancer Center, University of Pennsylvania, Philadelphia, Pennsylvania 191043

Received 27 November 2002/ Accepted 18 February 2003

Retrovirus infection is initiated by binding of the surface (SU) portion of the viral envelope glycoprotein (Env) to specific receptors on cells. This binding triggers conformational changes in the transmembrane portion of Env, leading to membrane fusion and cell entry, and is thus a major determinant of retrovirus tissue and species tropism. The M813 murine leukemia virus (MuLV) is a highly fusogenic gammaretrovirus, isolated from Mus cervicolor, whose host range is limited to mouse cells. To delineate the molecular mechanisms of its restricted host range and its high fusogenic potential, we initiated studies to characterize the cell surface protein that mediates M813 infection. Screening of the T31 mouse-hamster radiation hybrid panel for M813 infectivity localized the receptor gene to the distal end of mouse chromosome 16. Expression of one of the likely candidate genes (slc5a3) within this region in human cells conferred susceptibility to both M813 infection and M813-induced fusogenicity. slc5a3 encodes sodium myo-inositol transporter 1 (SMIT1), thus adding another sodium-dependent transporter to the growing list of proteins used by MuLVs for cell entry. Characterization of SMIT1 orthologues in different species identified several amino acid variations within two extracellular loops that may restrict susceptibility to M813 infection.

* Corresponding author. Mailing address: Heinrich-Pette-Institut, Martinistr. 52, D-20251 Hamburg, Germany. Phone: 49-40-480 51 273. Fax: 40-40-480 51 187. E-mail: stocking{at}hpi.uni-hamburg.de.

Journal of Virology, May 2003, p. 5926-5932, Vol. 77, No. 10
0022-538X/03/$08.00+0     DOI: 10.1128/JVI.77.10.5926-5932.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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