@article {711,
	title = {Simian virus 40 infection via MHC class I molecules and caveolae.},
	journal = {Immunol Rev},
	volume = {168},
	year = {1999},
	month = {1999 Apr},
	pages = {13-22},
	abstract = {MHC class I molecules are a necessary component of the cell surface receptor for simian virus 40 (SV40). After binding to class I molecules, SV40 enters cells via a unique endocytic pathway that involves caveolae, rather than clathrin-coated pits. This pathway is dependent on a transmembrane signal that SV40 transmits from the cell surface. Furthermore, it delivers SV40 to the endoplasmic reticulum, rather than to the endosomal/lysosomal compartment, which is the usual target for endocytic traffic. The glycosphingolipid and cholesterol-enriched plasma membrane domains that contain caveolae are also enriched for class I molecules, relative to whole plasma membrane. Nevertheless, although class I molecules bind SV40, they do not enter with SV40, nor do they enter spontaneously into uninfected SV40 host cells. Instead, they are shed from the cell surface by the activity of a metalloprotease. These results imply the existence of a putative secondary receptor for SV40 that might mediate SV40 entry. It is not yet clear whether class I molecules are active in transmitting the SV40 signal. Monoclonal antibodies against class I molecules also induce a signal in the SV40 host cells. However, the antibody-induced signal is mediated by mitogen-activated protein kinase (MAP kinase), whereas the SV40 signal is independent of MAP kinase.},
	keywords = {Animals, Cell Membrane, Histocompatibility Antigens Class I, Humans, Papillomavirus Infections, Receptors, Virus, Simian virus 40, Tumor Virus Infections},
	issn = {0105-2896},
	author = {Norkin, L C}
}
@article {709,
	title = {MHC class I molecules are enriched in caveolae but do not enter with simian virus 40.},
	journal = {J Gen Virol},
	volume = {79 ( Pt 6)},
	year = {1998},
	month = {1998 Jun},
	pages = {1469-77},
	abstract = {Simian virus 40 (SV40) binds to MHC class I molecules anywhere on the cell surface and then enters through caveolae. The fate of class I molecules after SV40 binding is not known. Sensitivity of 125I-surface-labelled class I molecules to papain cleavage was used to distinguish internalized class I molecules from class I molecules remaining at the cell surface. Whereas the caveolae-enriched membrane microdomain was found to also be enriched for class I molecules, no internalized papain-resistant 125I-surface-labelled class I molecules could be detected at any time in either control cells or in cells preadsorbed with saturating amounts of SV40. Instead, 125I-surface-labelled class I molecules, as well as preadsorbed 125I-labelled anti-class I antibodies, accumulated in the medium, coincident with the turnover of class I molecules at the cell surface. The class I heavy chains that accumulated in the medium were truncated and their release was specifically prevented by the metalloprotease inhibitor 1,10-phenanthroline. Thus, whereas class I molecules mediate SV40 binding, they do not appear to mediate SV40 entry.},
	keywords = {Animals, Caveolin 1, Caveolins, Cell Line, Cell Membrane, Cercopithecus aethiops, Histocompatibility Antigens Class I, Humans, Membrane Proteins, Simian virus 40},
	issn = {0022-1317},
	author = {Anderson, H A and Chen, Y and Norkin, L C}
}
@article {706,
	title = {Multiple stages of virus-receptor interactions as shown by simian virus 40.},
	journal = {Adv Exp Med Biol},
	volume = {408},
	year = {1996},
	month = {1996},
	pages = {159-67},
	keywords = {Animals, Cell Membrane, Histocompatibility Antigens Class I, Humans, Receptors, Virus, Signal Transduction, Simian virus 40},
	issn = {0065-2598},
	author = {Norkin, L C and Anderson, H A}
}
@article {703,
	title = {Class I major histocompatibility proteins are an essential component of the simian virus 40 receptor.},
	journal = {J Virol},
	volume = {66},
	year = {1992},
	month = {1992 Apr},
	pages = {2037-45},
	abstract = {The class I molecules encoded by the major histocompatibility complex (MHC) present endogenously synthesized antigenic peptide fragments to cytotoxic T lymphocytes. We show here that these proteins are an essential component of the cell surface receptor for simian virus 40 (SV40). First, SV40 binding to cells can be blocked by two monoclonal antibodies against class I human lymphocyte antigen (HLA) proteins but not by monoclonal antibodies specific for other cell surface proteins. Second, SV40 does not bind to cells of two different human lymphoblastoid cell lines which do not express surface class I MHC proteins because of genetic defects in the beta 2-microglobulin gene in one line and in the HLA complex in the other. Transfection of these cell lines with cloned genes for beta 2-microglobulin and HLA-B8, respectively, restored expression of their surface class I MHC proteins and resulted in concomitant SV40 binding. Finally, SV40 binds to purified HLA proteins in vitro and selectively binds to class I MHC proteins in a cell surface extract.},
	keywords = {Animals, Binding, Competitive, Blotting, Western, Cell Line, Flow Cytometry, Histocompatibility Antigens Class I, Humans, Precipitin Tests, Receptors, Virus, Simian virus 40, Transfection},
	issn = {0022-538X},
	author = {Breau, W C and Atwood, W J and Norkin, L C}
}
