Hydroxyproline in the major capsid protein VP1 of polyomavirus

Ludlow, John W.; Consigli, Richard A.

doi:10.1128/jvi.63.6.2881-2884.1989

Cited by 12 publications

(5 citation statements)

References 33 publications

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“…Removal of the chelator and reducing agent together with addition of CaCl2 resulted in the assembly of these capsomeres into structures which resembled viral capsids. Besides further implicating a role for calcium in maintaining the structural integrity of the virus, these studies also suggested that the posttranslational modifications of VP1 which occur in eukaryotic cells (2,3,5,18,19,26,28,29,35) may not be necessary for proper capsid formation. These studies also indicated that the minor capsid proteins were not necessary for in vitro assembly.…”

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confidence: 97%

Mutations in the putative calcium-binding domain of polyomavirus VP1 affect capsid assembly

Haynes

Chang

Consigli

1993

J Virol

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confidence: 97%

Mutations in the putative calcium-binding domain of polyomavirus VP1 affect capsid assembly

Haynes

Chang

Consigli

1993

J Virol

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“…The abundantly synthesized VP1 protein of polyomavirus has been reported to consist of six isoelectric species posttranslationally modified by phosphorylation and acetylation (3). VP1 has also been found to contain hydroxyproline (28). It has been proposed that differently modified VP1 species play a role in the attachment of virions to the cell surface and in the ability of viral particles to hemagglutinate erythrocytes (9).…”

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confidence: 99%

Cooperation of structural proteins during late events in the life cycle of polyomavirus

Forstová

Krauzewicz

Wallace

et al. 1993

J Virol

112

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The polyomavirus minor late capsid antigen, VP2, is myristylated on its N-terminal glycine, this modification being required for efficient infection of mouse cells. To study further the functions of this antigen, as well as those of the other minor late antigen, VP3, recombinant baculoviruses carrying genes for VP1, VP2, and VP3 have been constructed and the corresponding proteins have been synthesized in insect cells. A monoclonal antibody recognizing VP1, a-PyVP1-A, and two monoclonal antibodies against the common region of VP2 and VP3, at-PyVP2/3-A and at-PyVP2/3-B, have been generated. Reactions of antibodies with antigens were characterized by indirect immunofluorescence, immunoprecipitation, and immunoblot analysis. Immunofluorescent staining of mouse cells infected with polyomavirus showed all antigens to be localized in nuclei. When

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“…Different posttranslational modifications (PTMs) of the same polypeptide may serve different biological functions (Fang et al, 2010;Seo & Lee, 2004;Yan et al, 1998). The PTMs of VP1 of polyomavirus have been demonstrated to have crucial roles in the viral life cycle (Bolen & Consigli, 1979;Bolen et al, 1981;Garcea & Benjamin, 1983;Ludlow & Consigli, 1987a, 1989. SV40 VP1 can be separated into six species by isoelectric focusing and two species have been found to be phosphorylated (O'Farrell & Goodman, 1976;Ponder et al, 1977).…”

Section: Introductionmentioning

confidence: 99%

“…Species C and D have been identified as being acetylated (Bolen et al, 1981). Other modifications of VP1 include methylation and hydroxylation (Burton & Consigli, 1996;Ludlow & Consigli, 1989), with hydroxylation affecting the transportation of polyomavirus VP1 into the cell nucleus for assembly (Ludlow & Consigli, 1989).…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation of Ser-80 of VP1 and Ser-254 of VP2 is essential for human BK virus propagation in tissue culture

Chen

Hsu

Fang

et al. 2011

Journal of General Virology

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ROCBK virus (BKV) infection may cause polyomavirus-associated nephropathy in patients with renal transplantation. Recently, the phosphorylated amino acids on the structural proteins VP1, VP2 and VP3 of BKV have been identified by liquid chromatography-tandem mass spectrometry in our laboratory. In this study, we further analysed the biological effects of these phosphorylation events. Phosphorylation of the BKV structural proteins was demonstrated by [32 P]orthophosphate labelling in vivo. Site-directed mutagenesis was performed to replace all of the phosphorylated amino acids. The mutated BKV genomes were transfected into Vero cells for propagation analysis.The results showed that expression of the early protein LT and of the late protein VP1 by the mutants VP1-S80A, VP1-S80-133A, VP1-S80-327A, VP1-S80-133-327A and VP2-S254A was abolished. However, propagation of other mutants was similar to that of wild-type BKV. The results suggest that phosphorylation of Ser-80 of VP1 and Ser-254 of VP2 is crucial for BKV propagation. INTRODUCTIONPolyomaviruses are non-enveloped small DNA viruses and have a circular dsDNA genome of approximately 5.2 kbp. The polyomavirus family includes murine polyomavirus, simian virus (SV40), human John Cunningham virus (JCV), BK virus (BKV), KI virus, WU virus and Merkel cell polyomavirus (MCV) (Allander et al., 2007;Eash et al., 2006;Feng et al., 2008;Gardner et al., 1971;Gaynor et al., 2007;Kanitakis, 2008; Pérez-Losada et al., 2006). The genomes of these polyomaviruses contain regulatory, early and late regions. The regulatory region includes the replication origin as well as a promoter and an enhancer that regulate the transcription of the early and late genes. The early region encodes the regulatory proteins large tumour antigen (LT) and small tumour antigen, which are associated with replication and the regulation of the early and late genes. The late region encodes three structural capsid proteins, VP1, VP2 and VP3, and the regulatory agonoprotein (Safak et al., 2001). The viral capsid is composed of the major structural protein, VP1, the minor structural proteins, VP2 and VP3, and a viral minichromosome (Christiansen et al., 1977). The viral capsid consists of 72 pentameric capsomeres, including 12 pentavalent and 60 hexavalent capsomeres (Liddington et al., 1991).The structural proteins of polyomavirus play important roles in the infection life cycle, such as recognition of host receptors, haemagglutination activity (Bolen & Consigli, 1979;Bolen et al., 1981) and encapsidation of the viral genome during maturation (Chang et al., 1993;Gasparovic et al., 2006;Kawano et al., 2006). Furthermore, interactions among the structural proteins are also crucial for virus entry, nuclear translocation, DNA packaging and assembly of viral progeny (Chen et al., 1998;Delos et al., 1995;Gasparovic et al., 2006;Gharakhanian et al., 2003;Kawano et al., 2006;Shishido-Hara et al., 2004). However, it has been found that the structural proteins are modified into several subspecies, as demonstrated by t...

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Hydroxyproline in the major capsid protein VP1 of polyomavirus

Cited by 12 publications

References 33 publications

Mutations in the putative calcium-binding domain of polyomavirus VP1 affect capsid assembly

Mutations in the putative calcium-binding domain of polyomavirus VP1 affect capsid assembly

Cooperation of structural proteins during late events in the life cycle of polyomavirus

Phosphorylation of Ser-80 of VP1 and Ser-254 of VP2 is essential for human BK virus propagation in tissue culture

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