Mouse Transferrin Receptor 1 Is the Cell Entry Receptor for Mouse Mammary Tumor Virus

Enveloped viruses enter cells by binding to their entry receptors and fusing with the membrane at the cell surface or after trafficking through acidic endosomal compartments. Species-specific virus tropism is usually determined by these entry receptors. Because mouse mammary tumor virus (MMTV) is un...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2002-09, Vol.99 (19), p.12386-12390
Main Authors: Ross, Susan R., Schofield, Jason J., Farr, Christine J., Bucan, Maja
Format: Article
Language:English
Subjects:
Animals
Biological Sciences
Cell Line
Cell lines
Cell surface receptors
Cells
Chromosome Mapping
Chromosomes, Artificial, Bacterial - genetics
Cricetinae
Endosomes
Humans
Hybrid Cells
Infections
Mammary Tumor Virus, Mouse - pathogenicity
Mammary Tumor Virus, Mouse - physiology
Membranes
Mice
Microbiology
Proteins
Receptors
Receptors, Transferrin - genetics
Receptors, Transferrin - physiology
Receptors, Virus - genetics
Receptors, Virus - physiology
Somatic cells
Transfection
Transferrins
Tumors
Viruses
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Summary:Enveloped viruses enter cells by binding to their entry receptors and fusing with the membrane at the cell surface or after trafficking through acidic endosomal compartments. Species-specific virus tropism is usually determined by these entry receptors. Because mouse mammary tumor virus (MMTV) is unable to infect Chinese hamster cells, we used phenotypic screening of the T31 mouse/hamster radiation hybrid panel to map the MMTV cell entry receptor gene and subsequently found that it is transferrin receptor 1. MMTV-resistant human cells that expressed mouse transferrin receptor 1 became susceptible to MMTV infection, and treatment of mouse cells with a monoclonal antibody that down-regulated cell surface expression of the receptor blocked infection. MMTV, like vesicular stomatitis virus, depended on acid pH for infection. MMTV may use transferrin receptor 1, a membrane protein that is endocytosed via clathrin-coated pits and traffics through the acidic endosomes, to rapidly get to a compartment where acid pH triggers the conformational changes in envelope protein required for membrane fusion.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.192360099