title: Disassembly of simian virus 40 during passage through the endoplasmic reticulum and in the cytoplasm.
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.
authors.affiliation: Department of Microbiology, University of Massachusetts, Amherst, Massachusetts, USA.
authors.forename: Dmitry
authors.initials: D
authors.lastname: Kuksin
authors.forename: Leonard C
authors.initials: LC
authors.lastname: Norkin
mesh_terms: D000818:Animals; D002460:Cell Line; D002522:Chlorocebus aethiops; D003593:Cytoplasm / Q000821:virology*; D004721:Endoplasmic Reticulum / Q000821:virology*; D016679:Genome, Viral; D008856:Microscopy, Fluorescence; D013539:Simian virus 40 / Q000235:genetics / Q000502:physiology*; D019065:Virus Assembly
references.citation: Mol Biol Cell. 1996 Nov;7(11):1825-34
references.pmid: 8930903
references.citation: J Virol. 2007 Dec;81(23):12996-3004
references.pmid: 17881435
references.citation: Cell. 2007 Nov 2;131(3):516-29
references.pmid: 17981119
references.citation: EMBO J. 1998 Jun 15;17(12):3233-40
references.pmid: 9628860
references.citation: J Virol. 2006 Jul;80(13):6575-87
references.pmid: 16775344
references.citation: Proc Natl Acad Sci U S A. 1996 Jan 9;93(1):96-100
references.pmid: 8552683
references.citation: J Virol. 2002 May;76(10):5156-66
references.pmid: 11967331
references.citation: J Virol. 2004 Nov;78(21):11583-90
references.pmid: 15479799
references.citation: EMBO J. 2003 Sep 1;22(17):4346-55
references.pmid: 12941687
references.citation: J Virol. 2006 Sep;80(17):8739-44
references.pmid: 16912321
references.citation: Virology. 1993 Jan;192(1):142-53
references.pmid: 8390748
references.citation: Nat Cell Biol. 2001 May;3(5):473-83
references.pmid: 11331875
references.citation: Mol Cell. 2006 Dec 28;24(6):955-66
references.pmid: 17189196
references.citation: Virology. 1973 Oct;55(2):329-38
references.pmid: 4355111
references.citation: Nature. 1991 Nov 28;354(6351):278-84
references.pmid: 1659663
references.citation: Exp Cell Res. 1999 Jan 10;246(1):83-90
references.pmid: 9882517
references.citation: J Virol. 2003 Feb;77(3):1672-81
references.pmid: 12525601
references.citation: J Virol. 1992 Apr;66(4):2037-45
references.pmid: 1312619
references.citation: J Virol. 2002 Sep;76(18):9368-77
references.pmid: 12186919
references.citation: J Cell Biol. 1989 Dec;109(6 Pt 1):2721-9
references.pmid: 2556405
references.citation: J Virol. 2003 Jul;77(13):7527-38
references.pmid: 12805453
references.citation: mBio. 2011 Jun 14;2(3):e00101-11
references.pmid: 21673190
references.citation: Nat Rev Mol Cell Biol. 2008 Dec;9(12):944-57
references.pmid: 19002207
references.citation: J Virol. 2009 Feb;83(3):1350-8
references.pmid: 19036822
references.citation: J Virol. 2006 Jan;80(2):759-68
references.pmid: 16378978