Identification of phosphorylated residues on varicella-zoster virus immediate-early protein ORF63

Mueller, Niklaus H.; Walters, Matthew S.; Marcus, Randall E.; Graf, Laurie L.; Prenni, Jessica E.; Gilden, Don; Silverstein, Saul; Cohrs, Randall J.

doi:10.1099/vir.0.019067-0

Cited by 12 publications

(14 citation statements)

References 34 publications

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“…2B). The epitope for recMAb 63E4 maps to a site 36 amino acids C-terminal to the rec-MAb 63P4 epitope, and antibody binding to IE63 requires phosphorylation at S186 (24). These findings indicate that the VZV IE63 epitope recognized by rec-MAb 63P4 is blocked by a proline at 142 in SVV.…”

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confidence: 54%

“…VZV ORF63 encodes immediate-early 63 (IE63), a 278-amino-acid protein expressed early after VZV infection in cell culture (10). Phosphorylated IE63 is found predominantly in the nuclei of productively infected cells (4,9,23,24,27) but exclusively in the cytoplasms of latently infected human ganglia, where its function in maintaining latency and its posttranslational modification are unknown (21).Characterization of VZV IE63 cellular localization and protein interactions is critically dependent on the availability of well-defined antibodies. Previously, four anti-IE63 antibodies have been described: mouse monoclonal antibody (MAb) 9A12 (17), rabbit polyclonal anti-IE63 (R␣IE63) (10), recombinant MAb 63E4 (rec-MAb 63E4) (24), and rec-Ab 63P4 (22).…”

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confidence: 99%

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confidence: 99%

“…Previously, four anti-IE63 antibodies have been described: mouse monoclonal antibody (MAb) 9A12 (17), rabbit polyclonal anti-IE63 (R␣IE63) (10), recombinant MAb 63E4 (rec-MAb 63E4) (24), and rec-Ab 63P4 (22). Cellular localization of IE63 has been determined using both R␣IE63 and mouse MAb 9A12; however, concerns have recently arisen about detection of IE63 by immunohistochemistry, since intraneuronal deposition of lipofuscin and neuromelanin confounds analysis of IE63 in human trigeminal ganglia using rabbit anti-IE63 polyclonal antibodies (28).…”

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confidence: 99%

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Recombinant Monoclonal Antibody Recognizes a Unique Epitope on Varicella-Zoster Virus Immediate-Early 63 Protein

Mueller¹,

Bos²,

Seitz³

et al. 2012

J Virol

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We previously constructed a recombinant monoclonal antibody (rec-MAb 63P4) that detects immediate-early protein IE63 encoded by varicella-zoster virus (VZV) in the cytoplasm of productively infected cells. Here, we used ORF63 truncation mutants to map the rec-MAb 63P4 binding epitope to amino acids 141 to 150 of VZV IE63, a region not shared with other widely used anti-IE63 antibodies, and found that the recombinant antibody does not bind to the simian IE63 counterpart.

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confidence: 54%

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Recombinant Monoclonal Antibody Recognizes a Unique Epitope on Varicella-Zoster Virus Immediate-Early 63 Protein

Mueller¹,

Bos²,

Seitz³

et al. 2012

J Virol

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“…Tyrosine phosphorylation is involved in the replication of several herpesviruses (Geiss et al, 2001;Ren et al, 2001) and in shifting protein translocation from the cytoplasm to the nucleus during productive virus infection (Pomeranz and Blaho, 1999). Phosphorylation of VZV ORF63 is associated with its subcellular localization and transcriptional regulatory properties (Habran et al, 2005;Mueller et al, 2010), and phosphorylation of ICP22 is involved in HSV-1 virulence (Brandt and Kolb, 2003). Therefore, PICP22 phosphorylation may also play an important role during PRV infection, perhaps in modulating its subcellular localization or other uncharacterized functions, such as transcriptional regulation.…”

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confidence: 99%

Molecular cloning and characterization of the pseudorabies virus US1 gene

Chen

Zhao

et al. 2013

Genet. Mol. Res.

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ABSTRACT. Using polymerase chain reaction, a 1050-bp sequence of the US1 gene was amplified from the pseudorabies virus (PRV) Becker strain genome; identification of the US1 gene was confirmed by further cloning and sequencing. Bioinformatics analysis indicated that the PRV US1 gene encodes a putative polypeptide with 349 amino acids. The encoded protein, designated PICP22, had a conserved Herpes_IE68 domain, which was found to be closely related with the herpes virus immediate early regulatory protein family and is highly conserved among the counterparts encoded by Herpes_IE68 genes. Multiple nucleic acid sequence and amino acid sequence alignments suggested that the product of PRV US1 has a relatively higher homology with ICP22-like proteins of genus Varicellovirus than with those of other genera of Alphaherpesvirinae. In addition, phylogenetic analysis showed that PRV US1 has a close evolutionary relationship with members of the genus Varicellovirus, especially Equid herpes virus 1 (EHV-1), EHV-4 and EHV-9. Antigen prediction indicated that several potential B-cell epitopes are located in PICP22. Also, subcellular localization analysis demonstrated that PICP22 is predominantly located in the cytoplasm, suggesting that it might function as a cytoplasmic-targeted protein.

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Investigating the biology of alpha herpesviruses with MS‐based proteomics

et al. 2015

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Viruses are intracellular parasites that can only replicate and spread in cells of susceptible hosts. Alpha herpesviruses (α-HVs) contain double stranded DNA genomes of at least 120 kb, encoding for 70 or more genes. The viral genome is contained in an icosahedral capsid that is surrounded by a proteinaceous tegument layer and a lipid envelope. Infection starts in epithelial cells and spreads to the peripheral nervous system (PNS). In the natural host, α-HVs establish a chronic latent infection that can be reactivated, rarely spread to the central nervous system (CNS). In the non-natural host, viral infection will in most cases spread to the CNS with often fatal outcome. The host response plays a crucial role in the outcome of viral infection. α-HVs do not encode all the genes required for viral replication and spread. They need a variety of host gene products including RNA polymerase, ribosomes, dynein, and kinesin. As a result, the infected cell is dramatically different from the uninfected cell revealing a complex and dynamic interplay of viral and host components required to complete the virus life cycle. In this review, we describe the pivotal contribution of mass spectrometry-based proteomics (MSBP) studies over the past 15 years to understanding the complicated life cycle and pathogenesis of four α-HV species from the alphaherpesvirinae subfamily: Herpes simplex virus-1 (HSV-1), varicella zoster virus (VZV), pseudorabies virus (PRV) and bovine herpes virus (BHV-1). We describe the viral proteome dynamics during host infection and the host proteomic response to counteract such pathogens.

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Identification of phosphorylated residues on varicella-zoster virus immediate-early protein ORF63

Cited by 12 publications

References 34 publications

Recombinant Monoclonal Antibody Recognizes a Unique Epitope on Varicella-Zoster Virus Immediate-Early 63 Protein

Recombinant Monoclonal Antibody Recognizes a Unique Epitope on Varicella-Zoster Virus Immediate-Early 63 Protein

Molecular cloning and characterization of the pseudorabies virus US1 gene

Investigating the biology of alpha herpesviruses with MS‐based proteomics

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