ArticleJournal of virology2006
Identification of amino acid residues within simian virus 40 capsid proteins Vp1, Vp2, and Vp3 that are required for their interaction and for viral infection.
Article in Journal of virology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed.
- Immune Modulation by Microbiota and Its Possible Impact on Polyomavirus Infection.Pathogens (Basel, Switzerland) · 2025Review
- Revisiting JC virus and progressive multifocal leukoencephalopathy.Journal of neurovirology · 2023Review
- Article
- Formation of covalently modified folding intermediates of simian virus 40 Vp1 in large T antigen-expressing cells.Journal of virology · 2013Article
- The Simian virus 40 late viral protein VP4 disrupts the nuclear envelope for viral release.Journal of virology · 2012Article
- Pseudovirions as vehicles for the delivery of siRNA.Pharmaceutical research · 2010Article
- A very late viral protein triggers the lytic release of SV40.PLoS pathogens · 2007Article
- Minor capsid proteins of simian virus 40 are dispensable for nucleocapsid assembly and cell entry but are required for nuclear entry of the viral genome.Journal of virology · 2007Article
- A structural rationale for SV40 Vp1 temperature-sensitive mutants and their complementation.Protein science : a publication of the Protein Society · 2006Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Interaction of simian virus 40 (SV40) major capsid protein Vp1 with the minor capsid proteins Vp2 and Vp3 is an integral aspect of the SV40 architecture. Two Vp3 sequence elements mediate Vp1 pentamer binding in vitro, Vp3 residues 155 to 190, or D1, and Vp3 residues 222 to 234, or D2. Of the two, D1 but not D2 was necessary and sufficient to direct the interaction with Vp1 in vivo. Rational mutagenesis of Vp3 residues (Phe157, Ile158, Pro164, Gly165, Gly166, Leu177, and Leu181) or Vp1 residues (Val243 and Leu245), based on a structural model of the SV40 Vp1 pentamer complexed with Vp3 D1, was carried out to disrupt the interaction between Vp1 and Vp3 and to study the consequences of these mutations for viral viability. Altering these residues to bulky, charged residues blocked the interaction in vitro. When these alterations were introduced into the viral genome, they reduced viral viability. Mutants with alterations in Vp1 Val243, Leu245, or both to glutamate were nearly nonviable, whereas those with Vp3 alterations reduced, but did not eliminate, viability. Our results defined the residues of Vp1 and the minor capsid proteins that are essential for both the interaction of the capsid proteins and viral viability in permissive cells.
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