<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Simian virus 40 infection via MHC class I molecules and caveolae.</style></title><secondary-title><style face="normal" font="default" size="100%">Immunol Rev</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Immunol. Rev.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Histocompatibility Antigens Class I</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Papillomavirus Infections</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, Virus</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Tumor Virus Infections</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1999</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1999 Apr</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">168</style></volume><pages><style face="normal" font="default" size="100%">13-22</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">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.</style></abstract><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/10399061?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Norkin, L C</style></author><author><style face="normal" font="default" size="100%">Anderson, H A</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Multiple stages of virus-receptor interactions as shown by simian virus 40.</style></title><secondary-title><style face="normal" font="default" size="100%">Adv Exp Med Biol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Adv. Exp. Med. Biol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Membrane</style></keyword><keyword><style  face="normal" font="default" size="100%">Histocompatibility Antigens Class I</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, Virus</style></keyword><keyword><style  face="normal" font="default" size="100%">Signal Transduction</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1996</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1996</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">408</style></volume><pages><style face="normal" font="default" size="100%">159-67</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/8895788?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Virus receptors: implications for pathogenesis and the design of antiviral agents.</style></title><secondary-title><style face="normal" font="default" size="100%">Clin Microbiol Rev</style></secondary-title><alt-title><style face="normal" font="default" size="100%">Clin. Microbiol. Rev.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Antigens, CD4</style></keyword><keyword><style  face="normal" font="default" size="100%">Antiviral Agents</style></keyword><keyword><style  face="normal" font="default" size="100%">Coronavirus</style></keyword><keyword><style  face="normal" font="default" size="100%">Drug Design</style></keyword><keyword><style  face="normal" font="default" size="100%">Herpesviridae</style></keyword><keyword><style  face="normal" font="default" size="100%">HIV</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Intercellular Adhesion Molecule-1</style></keyword><keyword><style  face="normal" font="default" size="100%">Models, Molecular</style></keyword><keyword><style  face="normal" font="default" size="100%">Picornaviridae</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, Virus</style></keyword><keyword><style  face="normal" font="default" size="100%">Retroviridae</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1995</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1995 Apr</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">8</style></volume><pages><style face="normal" font="default" size="100%">293-315</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">A virus initiates infection by attaching to its specific receptor on the surface of a susceptible host cell. This prepares the way for the virus to enter the cell. Consequently, the expression of the receptor on specific cells and tissues of the host is a major determinant of the route of entry of the virus into the host and of the patterns of virus spread and pathogenesis in the host. This review emphasizes the virus-receptor interactions of human immunodeficiency virus, the rhinoviruses, the herpesviruses, and the coronaviruses. These interactions are often found to be complex and dynamic, involving multiple sites or factors on both the virus and the host cell. Also, the receptor may play an important role in virus entry per se in addition to its role in virus binding. In the cases of human immunodeficiency virus and the rhinoviruses, ingenious approaches to therapeutic strategies based on inhibiting virus attachment and entry are under development and in clinical trials.</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/7621403?dopt=Abstract</style></custom1></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Breau, W C</style></author><author><style face="normal" font="default" size="100%">Atwood, W J</style></author><author><style face="normal" font="default" size="100%">Norkin, L C</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Class I major histocompatibility proteins are an essential component of the simian virus 40 receptor.</style></title><secondary-title><style face="normal" font="default" size="100%">J Virol</style></secondary-title><alt-title><style face="normal" font="default" size="100%">J. Virol.</style></alt-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Animals</style></keyword><keyword><style  face="normal" font="default" size="100%">Binding, Competitive</style></keyword><keyword><style  face="normal" font="default" size="100%">Blotting, Western</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell Line</style></keyword><keyword><style  face="normal" font="default" size="100%">Flow Cytometry</style></keyword><keyword><style  face="normal" font="default" size="100%">Histocompatibility Antigens Class I</style></keyword><keyword><style  face="normal" font="default" size="100%">Humans</style></keyword><keyword><style  face="normal" font="default" size="100%">Precipitin Tests</style></keyword><keyword><style  face="normal" font="default" size="100%">Receptors, Virus</style></keyword><keyword><style  face="normal" font="default" size="100%">Simian virus 40</style></keyword><keyword><style  face="normal" font="default" size="100%">Transfection</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">1992</style></year><pub-dates><date><style  face="normal" font="default" size="100%">1992 Apr</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">66</style></volume><pages><style face="normal" font="default" size="100%">2037-45</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">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.</style></abstract><issue><style face="normal" font="default" size="100%">4</style></issue><custom1><style face="normal" font="default" size="100%">http://www.ncbi.nlm.nih.gov/pubmed/1312619?dopt=Abstract</style></custom1></record></records></xml>