@article {720,
	title = {Disassembly of simian virus 40 during passage through the endoplasmic reticulum and in the cytoplasm.},
	journal = {J Virol},
	volume = {86},
	year = {2012},
	month = {2012 Feb},
	pages = {1555-62},
	abstract = {The nonenveloped polyomavirus simian virus 40 (SV40) is taken up into cells by a caveola-mediated endocytic process that delivers the virus to the endoplasmic reticulum (ER). Within the ER lumen, the capsid undergoes partial disassembly, which exposes its internal capsid proteins VP2 and VP3 to immunostaining with antibodies. We demonstrate here that the SV40 genome does not become accessible to detection while the virus is in the ER. Instead, the genome becomes accessible two distinct detection procedures, one using anti-bromodeoxyuridine antibodies and the other using a 5-ethynyl-2-deoxyuridine-based chemical reaction, only after the emergence of partially disassembled SV40 particles in the cytoplasm. These cytoplasmic particles retain some of the SV40 capsid proteins, VP1, VP2, and VP3, in addition to the viral genome. Thus, SV40 particles undergo discrete disassembly steps during entry that are separated temporally and topologically. First, a partial disassembly of the particles occurs in the ER, which exposes internal capsid proteins VP2 and VP3. Then, in the cytoplasm, disassembly progresses further to also make the genomic DNA accessible to immune detection.},
	keywords = {Animals, Cell Line, Cercopithecus aethiops, Cytoplasm, Endoplasmic Reticulum, Genome, Viral, Microscopy, Fluorescence, Simian virus 40, Virus Assembly},
	issn = {1098-5514},
	doi = {10.1128/JVI.05753-11},
	author = {Kuksin, Dmitry and Norkin, Leonard C}
}
@article {721,
	title = {Disassociation of the SV40 Genome from Capsid Proteins Prior to Nuclear Entry.},
	journal = {Virol J},
	volume = {9},
	year = {2012},
	month = {2012 Aug 10},
	pages = {158},
	abstract = {ABSTRACT: BACKGROUND: Previously, we demonstrated that input SV40 particles undergo a partial disassembly in the endoplasmic reticulum, which exposes internal capsid proteins VP2 and VP3 to immunostaining. Then, in the cytoplasm, disassembly progresses further to also make the genomic DNA accessible to immune detection, as well as to detection by an ethynyl-2-deoxyuridine (EdU)-based chemical reaction. The cytoplasmic partially disassembled SV40 particles retain some of the SV40 capsid proteins, VP1, VP2, and VP3, in addition to the viral genome. FINDINGS: In the current study, we asked where in the cell the SV40 genome might disassociate from capsid components. We observed partially disassembled input SV40 particles around the nucleus and, beginning at 12 hours post-infection, 5-Bromo-2-deoxyuridine (BrdU)-labeled parental SV40 DNA in the nucleus, as detected using anti-BrdU antibodies. However, among the more than 1500 cells examined, we never detected input VP2/VP3 in the nucleus. Upon translocation of the BrdU-labeled SV40 genomes into nuclei, they were transcribed and, thus, are representative of productive infection CONCLUSIONS: Our findings imply that the SV40 genome disassociates from the capsid proteins before or at the point of entry into the nucleus, and then enters the nucleus devoid of VP2/3..},
	issn = {1743-422X},
	doi = {10.1186/1743-422X-9-158},
	author = {Kuksin, Dmitry and Norkin, Leonard C}
}
@article {719,
	title = {Taxonomical developments in the family Polyomaviridae.},
	journal = {Arch Virol},
	volume = {156},
	year = {2011},
	month = {2011 Sep},
	pages = {1627-34},
	abstract = {The Polyomaviridae Study Group of the International Committee on Taxonomy of Viruses (ICTV) has recommended several taxonomical revisions, as follows: The family Polyomaviridae, which is currently constituted as a single genus (Polyomavirus), will be comprised of three genera: two containing mammalian viruses and one containing avian viruses. The two mammalian genera will be designated Orthopolyomavirus and Wukipolyomavirus, and the avian genus will be named Avipolyomavirus. These genera will be created by the redistribution of species from the current single genus (Polyomavirus) and by the inclusion of several new species. In addition, the names of several species will be changed to reflect current usage.},
	keywords = {Phylogeny, Polyomaviridae, Terminology as Topic},
	issn = {1432-8798},
	doi = {10.1007/s00705-011-1008-x},
	author = {Johne, Reimar and Buck, Christopher B and Allander, Tobias and Atwood, Walter J and Garcea, Robert L and Imperiale, Michael J and Major, Eugene O and Ramqvist, Torbjorn and Norkin, Leonard C}
}
@article {718,
	title = {Simian virus 40 late proteins possess lytic properties that render them capable of permeabilizing cellular membranes.},
	journal = {J Virol},
	volume = {80},
	year = {2006},
	month = {2006 Jul},
	pages = {6575-87},
	abstract = {Many nonenveloped viruses have evolved an infectious cycle that culminates in the lysis or permeabilization of the host to enable viral release. How these viruses initiate the lytic event is largely unknown. Here, we demonstrated that the simian virus 40 progeny accumulated at the nuclear envelope prior to the permeabilization of the nuclear, endoplasmic reticulum, and plasma membranes at a time which corresponded with the release of the progeny. The permeabilization of these cellular membranes temporally correlated with late protein expression and was not observed upon the inhibition of their synthesis. To address whether one or more of the late proteins possessed an inherent capacity to induce membrane permeabilization, we examined the permeability of Escherichia coli that separately expressed the late proteins. VP2 and VP3, but not VP1, caused the permeabilization of bacterial membranes. Additionally, VP3 expression resulted in bacterial cell lysis. These findings demonstrate that VP3 possesses an inherent lytic property that is independent of eukaryotic signaling or cell death pathways.},
	keywords = {Animals, Capsid Proteins, Cell Death, Cell Line, Cell Membrane Permeability, Cercopithecus aethiops, Endoplasmic Reticulum, Escherichia coli, Gene Expression Regulation, Viral, Nuclear Envelope, Permeability, Protein Biosynthesis, Simian virus 40, Virus Replication},
	issn = {0022-538X},
	doi = {10.1128/JVI.00347-06},
	author = {Daniels, Robert and Rusan, Nasser M and Wilbuer, Anne-Kathrin and Norkin, Leonard C and Wadsworth, Patricia and Hebert, Daniel N}
}
@article {717,
	title = {The caveolae-mediated sv40 entry pathway bypasses the golgi complex en route to the endoplasmic reticulum.},
	journal = {Virol J},
	volume = {2},
	year = {2005},
	month = {2005},
	pages = {38},
	abstract = {BACKGROUND: Simian virus 40 (SV40) enters cells via an atypical caveolae-mediated endocytic pathway, which delivers the virus to a new intermediary compartment, the caveosome. The virus then is believed to go directly from the caveosome to the endoplasmic reticulum. Cholera toxin likewise enters via caveolae and traffics to caveosomes. But, in contrast to SV40, cholera toxin is transported from caveosomes to the endoplasmic reticulum via the Golgi. For that reason, and because the caveosome and Golgi may have some common markers, we revisited the issue of whether SV40 might access the endoplasmic reticulum via the Golgi.

RESULTS: We confirmed our earlier finding that SV40 co localizes with the Golgi marker beta-COP. However, we show that the virus does not co localize with the more discriminating Golgi markers, golgin 97 and BODIPY-ceramide.

CONCLUSION: The caveolae-mediated SV40 entry pathway does not intersect the Golgi. SV40 is seen to co localize with beta-COP because that protein is a marker for caveosomes as well as the Golgi. Moreover, these results are consistent with the likelihood that the caveosome is a sorting organelle. In addition, there are at least two distinct but related routes by which a ligand might traffic from the caveosome to the ER; one route involving transport through the Golgi, and another pathway that does not involve the Golgi.},
	keywords = {Animals, Caveolae, Cercopithecus aethiops, Endoplasmic Reticulum, Fibroblasts, Golgi Apparatus, Immunohistochemistry, Simian virus 40},
	issn = {1743-422X},
	doi = {10.1186/1743-422X-2-38},
	author = {Norkin, Leonard C and Kuksin, Dmitry}
}
@article {716,
	title = {Caveolin-2 associates with intracellular chlamydial inclusions independently of caveolin-1.},
	journal = {BMC Infect Dis},
	volume = {4},
	year = {2004},
	month = {2004 Jul 22},
	pages = {23},
	abstract = {BACKGROUND: Lipid raft domains form in plasma membranes of eukaryotic cells by the tight packing of glycosphingolipids and cholesterol. Caveolae are invaginated structures that form in lipid raft domains when the protein caveolin-1 is expressed. The Chlamydiaceae are obligate intracellular bacterial pathogens that replicate entirely within inclusions that develop from the phagocytic vacuoles in which they enter. We recently found that host cell caveolin-1 is associated with the intracellular vacuoles and inclusions of some chlamydial strains and species, and that entry of those strains depends on intact lipid raft domains. Caveolin-2 is another member of the caveolin family of proteins that is present in caveolae, but of unknown function.

METHODS: We utilized a caveolin-1 negative/caveolin-2 positive FRT cell line and laser confocal immunofluorescence techniques to visualize the colocalization of caveolin-2 with the chlamydial inclusions.

RESULTS: We show here that in infected HeLa cells, caveolin-2, as well as caveolin-1, colocalizes with inclusions of C. pneumoniae (Cp), C. caviae (GPIC), and C. trachomatis serovars E, F and K. In addition, caveolin-2 also associates with C. trachomatis serovars A, B and C, although caveolin-1 did not colocalize with these organisms. Moreover, caveolin-2 appears to be specifically, or indirectly, associated with the pathogens at the inclusion membranes. Using caveolin-1 deficient FRT cells, we show that although caveolin-2 normally is not transported out of the Golgi in the absence of caveolin-1, it nevertheless colocalizes with chlamydial inclusions in these cells. However, our results also show that caveolin-2 did not colocalize with UV-irradiated Chlamydia in FRT cells, suggesting that in these caveolin-1 negative cells, pathogen viability and very likely pathogen gene expression are necessary for the acquisition of caveolin-2 from the Golgi.

CONCLUSION: Caveolin-2 associates with the chlamydial inclusion independently of caveolin-1. The function of caveolin-2, either in the uninfected cell or in the chlamydial developmental cycle, remains to be elucidated. Nevertheless, this second caveolin protein can now be added to the small number of host proteins that are associated with the inclusions of this obligate intracellular pathogen.},
	keywords = {Animals, Blotting, Western, Caveolin 1, Caveolin 2, Caveolins, Cells, Cultured, Chlamydia, Fluorescent Antibody Technique, Golgi Apparatus, Guinea Pigs, HeLa Cells, Humans, Mice, Microscopy, Confocal, Rats, Vacuoles, Virulence},
	issn = {1471-2334},
	doi = {10.1186/1471-2334-4-23},
	author = {Webley, Wilmore C and Norkin, Leonard C and Stuart, Elizabeth S}
}
@article {715,
	title = {Lipid rafts, caveolae, caveolin-1, and entry by Chlamydiae into host cells.},
	journal = {Exp Cell Res},
	volume = {287},
	year = {2003},
	month = {2003 Jul 1},
	pages = {67-78},
	abstract = {Obligate intracellular bacterial pathogens of the genus Chlamydia are reported to enter host cells by both clathrin-dependent and clathrin-independent processes. C. trachomatis serovar K recently was shown to enter cells via caveolae-like lipid raft domains. We asked here how widespread raft-mediated entry might be among the Chlamydia. We show that C. pneumoniae, an important cause of respiratory infections in humans that additionally is associated with cardiovascular disease, and C. psittaci, an important pathogen in domestic mammals and birds that also infects humans, each enter host cells via cholesterol-rich lipid raft microdomains. Further, we show that C. trachomatis serovars E and F also use these domains to enter host cells. The involvement of these membrane domains in the entry of these organisms was indicated by the sensitivity of their entry to the raft-disrupting agents Nystatin and filipin, and by their intracellular association with caveolin-1, a 22-kDa protein associated with the formation of caveolae in rafts. In contrast, caveolin-marked lipid raft domains do not mediate entry of C. trachomatis serovars A, 36B, and C, nor of LGV serovar L2 and MoPn. Finally, we show that entry of each of these chlamydial strains is independent of cellular expression of caveolin-1. Thus, entry via the Nystatin and filipin-sensitive pathway is dependent on lipid rafts containing cholesterol, rather than invaginated caveolae per se.},
	keywords = {Anti-Bacterial Agents, Caveolae, Caveolin 1, Caveolins, Chlamydia, Chlamydia Infections, Cholesterol, Dose-Response Relationship, Drug, Eukaryotic Cells, Filipin, HeLa Cells, Host-Parasite Interactions, Humans, Membrane Microdomains, Nystatin, Species Specificity},
	issn = {0014-4827},
	author = {Stuart, Elizabeth S and Webley, Wilmore C and Norkin, Leonard C}
}
@article {714,
	title = {Caveolar endocytosis of simian virus 40 is followed by brefeldin A-sensitive transport to the endoplasmic reticulum, where the virus disassembles.},
	journal = {J Virol},
	volume = {76},
	year = {2002},
	month = {2002 May},
	pages = {5156-66},
	abstract = {Simian virus 40 (SV40) enters cells by atypical endocytosis mediated by caveolae that transports the virus to the endoplasmic reticulum (ER) instead of to the endosomal-lysosomal compartment, which is the usual destination for viruses and other cargo that enter by endocytosis. We show here that SV4O is transported to the ER via an intermediate compartment that contains beta-COP, which is best known as a component of the COPI coatamer complexes that are required for the retrograde retrieval pathway from the Golgi to the ER. Additionally, transport of SV40 to the ER, as well as infection, is sensitive to brefeldin A. This drug acts by specifically inhibiting the ARF1 GTPase, which is known to regulate assembly of COPI coat complexes on Golgi cisternae. Moreover, some beta-COP colocalizes with intracellular caveolin-1, which was previously shown to be present on a new organelle (termed the caveosome) that is an intermediate in the transport of SV40 to the ER (L. Pelkmans, J. Kartenbeck, and A. Helenius, Nat. Cell Biol. 3:473-483, 2001). We also show that the internal SV40 capsid proteins VP2 and VP3 become accessible to immunostaining starting at about 5 h. Most of that immunostaining overlays the ER, with some appearing outside of the ER. In contrast, immunostaining with anti-SV40 antisera remains confined to the ER.},
	keywords = {Animals, Antiviral Agents, Biological Transport, Brefeldin A, Capsid, Caveolae, Coatomer Protein, Endocytosis, Endoplasmic Reticulum, Simian virus 40, Virus Replication},
	issn = {0022-538X},
	author = {Norkin, Leonard C and Anderson, Howard A and Wolfrom, Scott A and Oppenheim, Ariella}
}
