ArticleProceedings of the National Academy of Sciences of the United States of America2002
Formation of transitory intrachain and interchain disulfide bonds accompanies the folding and oligomerization of simian virus 40 Vp1 in the cytoplasm.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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43 citing papers in PubMed, 65 citations in OpenAlex.
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- Host-membrane interacting interface of the SARS coronavirus envelope protein: Immense functional potential of C-terminal domain.Biophysical chemistry · 2020Review
- pH stability and disassembly mechanism of wild-type simian virus 40.Soft matter · 2020Article
- Empty SV40 capsids increase survival of septic rats by eliciting numerous host signaling networks that participate in a number of systemic functions.Oncotarget · 2020Article
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- Roles for human papillomavirus type 16 l1 cysteine residues 161, 229, and 379 in genome encapsidation and capsid stability.PloS one · 2014Article
- Scaffold properties are a key determinant of the size and shape of self-assembled virus-derived particles.ACS chemical biology · 2013Article
- Validated near-atomic resolution structure of bacteriophage epsilon15 derived from cryo-EM and modeling.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
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- Formation of covalently modified folding intermediates of simian virus 40 Vp1 in large T antigen-expressing cells.Journal of virology · 2013Article
- Biochemical and biophysical characterization of recombinant yeast proteasome maturation factor ump1.Computational and structural biotechnology journal · 2013Article
- Cysteine residues in the major capsid protein, Vp1, of the JC virus are important for protein stability and oligomer formation.PloS one · 2013Article
- Principles of polyoma- and papillomavirus uncoating.Medical microbiology and immunology · 2012Review
- RNA encapsidation by SV40-derived nanoparticles follows a rapid two-state mechanism.Journal of the American Chemical Society · 2012Article
- The C-terminal cysteine annulus participates in auto-chaperone function for Salmonella phage P22 tailspike folding and assembly.Bacteriophage · 2012Article
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4 authors at 1 institution in 1 country.
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Abstract
Pentamer formation by Vp1, the major capsid protein of simian virus 40, requires an interdigitation of structural elements from the Vp1 monomers [Liddington, R. C., Yan, Y., Moulai, J., Sahli, R., Benjamin, T. L. & Harrison, S. C. (1991) Nature (London) 354, 278-284]. Our analyses reveal that disulfide-linked Vp1 homooligomers are present in the simian virus 40-infected cytoplasm and that they are derived from a 41-kDa monomeric intermediate containing an intrachain disulfide bond(s). The 41-kDa species, emerging within 5 min of pulse labeling with [(35)S]methionine, is converted into a 45-kDa, disulfide-free Vp1 monomer and disulfide-bonded dimers through pentamers. The covalent oligomer formation is blocked in the presence of a sulfhydryl-modifying reagent. We propose that there are two stages in this Vp1 disulfide bonding. First, the newly synthesized Vp1 monomers acquire intrachain bonds as they fold and begin to interact. Next, these bonds are replaced with intermolecular bonds as the monomers assemble into pentamers. This sequential appearance of transitory disulfide bonds is consistent with a role for sulfhydryl-disulfide redox reactions in the coordinate folding of Vp1 chains into pentamers. The cytoplasmic Vp1 does not colocalize with marker proteins of the endoplasmic reticulum. This paper demonstrates in vivo disulfide formations and exchanges coupled to the folding and oligomerization of a mammalian protein in the cytoplasm, outside the secretory pathway. Such disulfide dynamics may be a general phenomenon for other cysteine-bearing mammalian proteins that fold in the cytoplasm.
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