@article {713,
	title = {Caveolae in the uptake and targeting of infectious agents and secreted toxins.},
	journal = {Adv Drug Deliv Rev},
	volume = {49},
	year = {2001},
	month = {2001 Jul 28},
	pages = {301-15},
	abstract = {A variety of microbial pathogens, including viruses, intracellular bacteria, and prions, as well as certain secreted bacterial toxins, can now be added to the list of ligands that enter cells via caveolae or caveolae-like membrane domains. In general, the caveolae-mediated entry pathway results in transport of these microbes and toxins to intracellular destinations that are different from that of cargo entering by other means. As a result, the caveolae-mediated entry pathway can profoundly affect the host cell-pathogen interaction long after entry has occurred. Furthermore, some microbes such as SV40 that enter via cavolae will be valuable as probes to analyze certain poorly understood intracellular trafficking pathways, such as retrograde transport to the ER. Also, viruses that enter via caveolae may have unique potential as gene and drug delivery vectors. In addition, some extracellular microbial pathogens, such as Pneumocystis carinii, may also interact with host cells via caveolae. Finally, caveolae may play a role in host immune defense mechanisms.},
	keywords = {Animals, Bacterial Infections, Caveolae, Humans, Toxins, Biological, Virus Diseases},
	issn = {0169-409X},
	author = {Norkin, L C}
}
@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}
}
