Biophysical characterization of polyomavirus minor capsid proteins

Burkert, Oliver; Kreßner, Susanne; Sinn, Ludwig; Giese, Sven; Simon, Claudia; Lilie, Hauke

doi:10.1515/hsz-2014-0114

Cited by 7 publications

(5 citation statements)

References 12 publications

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“…The hydrophobic helix was shown to be responsible for interactions of VP2 and VP3 with VP1 pentamers . In addition, computer analysis and circular dichroism spectroscopy of MPyV VP2 and VP3 have revealed that both proteins are highly hydrophobic with a high α‐helical content . In agreement, the viroporins described so far are proteins that contain one or several α‐helices that work as transmembrane domains .…”

Section: Introductionmentioning

confidence: 72%

Hydrophobic domains of mouse polyomavirus minor capsid proteins promote membrane association and virus exit from the ER

et al. 2017

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The minor structural protein VP2 and its shorter variant, VP3, of mouse polyomavirus (MPyV) are essential for virus exit from the endoplasmic reticulum (ER) during viral trafficking to the nucleus. Here, we followed the role of putative hydrophobic domains (HD) of the minor proteins in membrane affinity and viral infectivity. We prepared variants of VP2, each mutated to decrease hydrophobicity of one of three predicted hydrophobic domains: VP2-mHD1, VP2-mHD2 or VP2-mHD3 mutated in HD1 (amino acids (aa) 60-101), HD2 (aa 125-165) or HD3 (aa 287-307), respectively. Transient production of the mutated proteins revealed that only VP2-mHD2 lost the affinity for intracellular membranes. Cytotoxicity connected with the ability of VP2/VP3 to perforate membranes decreased markedly for VP2-mHD2, but only slightly for VP2-mHD1. The mutant VP2-mHD3 exhibited properties similar to the wild-type protein. MPyV genomes, each carrying one of the mutations, were prepared for virus production. MPyV-mHD1 and MPyVmHD2 viruses could be isolated, while the HD3 mutation in VP2/VP3 prevented virus assembly. We found that both MPyV-mHD1 and MPyV-mHD2 viruses arrived at the ER without delay and were processed by ER residential enzymes. However, the ability to associate with ER membranes was decreased in the case of MPyV-mHD1 and practically abolished in the case of MPyV-mHD2. Interestingly, while MPyV-mHD2 was not infectious, infection of MPyV-mHD1 virus was delayed. These findings reveal that HD2, common to both VP2 and VP3, is responsible for the membrane binding properties of the minor proteins, while HD1 of VP2 is likely required to stabilize VP2-membrane association and to enhance viral exit from the ER.

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Section: Introductionmentioning

confidence: 72%

Hydrophobic domains of mouse polyomavirus minor capsid proteins promote membrane association and virus exit from the ER

et al. 2017

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“…It might be debated whether JCPyV VP2 can be recognized by the immune system as it was proposed that VP2 is located at the inner side of the capsid [ 42 ]. Crystal structure analysis however showed that the N-terminal part of VP2, including the JCPyV_VP2_167-15mer region is not tightly folded and retains high flexibility, making it easier for VP2 to emerge from inside the virion [ 43 , 44 ]. The fact that it was also shown that 52.3% of serum samples show immunoreactivity with WU Polyomavirus VP2 and 21.9% of blood donors react with SV40 VP2 derived peptides, strengthens the conclusion that JCPyV VP2 acts as an antigen recognized by the immune system upon JCPyV infection [ 26 , 27 ].…”

Section: Resultsmentioning

confidence: 99%

Antibodies reacting with JCPyV_VP2 _167-15mer as a novel serological marker for JC polyomavirus infection

Lagatie

Loy

Tritsmans

et al. 2014

Virol J

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BackgroundJC polyomavirus (JCPyV) is a widespread human polyomavirus that usually resides latently in its host, but can be reactivated under immune-compromised conditions potentially causing Progressive Multifocal Leukoencephalopathy (PML). Detection of antibodies against the major capsid protein VP1 currently is the main marker for assessment of infection with JCPyV.MethodsBased on a peptide microarray, peptide JCPyV_VP2_167-15mer was selected and a peptide ELISA was developed for detection of antibodies directed against this peptide. Epitope mapping and computational modelling was performed to further characterize this peptide. In a cohort of 204 healthy subjects it was investigated whether antibodies against JCPyV_VP2_167-15mer were correlated with VP1 serology or urinary viral load.ResultsEpitope mapping of peptide JCPyV_VP2_167-15mer showed that the minimal epitope consisted of L173PALTSQEI181 with amino acids P174, L176 and E180 being essential for antibody recognition. Computational analysis was used to predict that this epitope is located at an exposed domain of the VP2 capsid protein, readily accessible for immune recognition upon infection. No correlation could be observed with JCPyV VP1 antibody levels, or urinary viral load.ConclusionThis work indicates that specific antibodies against JCPyV_VP2_167-15mer might be considered as a novel serological marker for infection with JCPyV.Electronic supplementary materialThe online version of this article (doi:10.1186/1743-422X-11-174) contains supplementary material, which is available to authorized users.

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“…The participation of agno-protein in viral evolution has been demonstrate in species which express these proteins, including, SV40, JCPyV and BKPyV (Saribas et al, 2016). Study conducted in the previous two decades have exhibits that the expression of VP1 in differ systems promote to the production of structures known as virus -like particles(VLPs), which are same as the viral capsid (Burkert et al, 2014;Touze et al, 2010). After it has expressed, the structural proteins assembled in the cellular nucleus, contributing to the observing of the virion.…”

Section: Biology Polyomavirusmentioning

confidence: 99%

Characteristics, transmission and pathogenesis of human Polyomavirus: A Review

Mahmood¹,

Ibrahim²,

Tiwari³

2021

Adv Pharm J

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The family Polyomaviridae contain about a number of human polyomaviruses (HPyVs), of which JCV, MCPyV, SV-40 and BKV viruses have been reported to cause many types of cancer in human. Merkel cell carcinoma is a very antagonistic type of skin cancer caused by the MCPyV5. Similarly, while JCV and SV-40 viruses developed brain tumour cancer, the BK virus has been bind to renal transplantations, prostate cancer and nephropathy producing urinary bladder tumor in human. The name of the family Polyomaviridae, derives from the observation that cells infected with murine polyomavirus produced multiple (poly) tumor (omas) in immune compromised mice. Although, present proof only supports to the role of MCPyV as a carcinogen in to the humans. In the present review we present a summarized discussion on the current knowledge regarding the role of JCPyV, TSPyV, BKPyV and MCPyV in human cancers.

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Biophysical characterization of polyomavirus minor capsid proteins

Cited by 7 publications

References 12 publications

Hydrophobic domains of mouse polyomavirus minor capsid proteins promote membrane association and virus exit from the ER

Hydrophobic domains of mouse polyomavirus minor capsid proteins promote membrane association and virus exit from the ER

Antibodies reacting with JCPyV_VP2 _167-15mer as a novel serological marker for JC polyomavirus infection

Characteristics, transmission and pathogenesis of human Polyomavirus: A Review

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