Sodium-Dependent myo -Inositol Transporter 1 Is a Cellular Receptor for Mus cervicolor M813 Murine Leukemia Virus
Autor: | Carol Stocking, Susan R. Ross, Jürgen Löhler, Dmitry Ivanov, Vladimir S. Prassolov, Sibyll Hein, Yuanming Zhang |
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Rok vydání: | 2003 |
Předmět: |
Molecular Sequence Data
Immunology Giant Cells Microbiology Chromosomes Cell Line Mice Retrovirus Viral envelope Cricetinae Virology Murine leukemia virus Animals Humans Amino Acid Sequence Heat-Shock Proteins Tropism Gammaretrovirus Symporters biology Chromosome Mapping Membrane Proteins biology.organism_classification Molecular biology Transmembrane protein Rats Virus-Cell Interactions Leukemia Virus Murine Muridae Membrane protein Cell culture Insect Science Receptors Virus |
Zdroj: | Journal of Virology. 77:5926-5932 |
ISSN: | 1098-5514 0022-538X |
DOI: | 10.1128/jvi.77.10.5926-5932.2003 |
Popis: | 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. |
Databáze: | OpenAIRE |
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