@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 {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}
}
