Viral protein kinases and protein phosphatases

Leader, David P.

doi:10.1016/0163-7258(93)90075-o

Cited by 48 publications

(35 citation statements)

References 219 publications

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“…These observations imply that the phosphorylation status of EA-D is probably important for its functions. The results suggest that EA-D is probably phosphorylated by an induced protein kinase, presumably viral, and that 1263W94 inhibits EBV replication at least partially through its effect on hyperphosphorylated EA-D. Beta-and gammaherpesviruses (including EBV) encode only one protein kinase (23) that is homologous to HSV UL13. UL13 has been shown to mediate the phosphorylation of viral proteins (such as ICP22 [30], gE and gI [26], and ICP0 [27]) and cellular factors (such as translation elongation factor 1 delta [20] and p60 [6]), thereby affecting viral replication and pathogenesis.…”

Section: Discussionmentioning

confidence: 94%

“…140-H, 1998), the product of which is a phosphotransferase (16,34,36). Homologs of this protein are encoded by all known herpesviruses; they contain conserved cyclic AMP-dependent protein kinase key catalytic residues (23). Protein kinase activity has already been demonstrated for HSV-1 UL13 (30), VZV ORF47 (25), and HCMV UL97 (16) and recently for EBV BGLF4 (7,18).…”

mentioning

confidence: 99%

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Phosphorylation of the Epstein-Barr Virus (EBV) DNA Polymerase Processivity Factor EA-D by the EBV-Encoded Protein Kinase and Effects of the l -Riboside Benzimidazole 1263W94

Gershburg

Pagano

2002

J Virol

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Section: Discussionmentioning

confidence: 94%

mentioning

confidence: 99%

Phosphorylation of the Epstein-Barr Virus (EBV) DNA Polymerase Processivity Factor EA-D by the EBV-Encoded Protein Kinase and Effects of the l -Riboside Benzimidazole 1263W94

Gershburg

Pagano

2002

J Virol

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“…We have shown here that p32 was a component of primary enveloped virions, which would enable p32 to interact with UL31 and the cytoplasmic domain of gB, which contains the Us3 phosphorylation site in primary enveloped virions. Interestingly, p32 is known to bind to arginine-rich regions of its target proteins (46) and the consensus Us3 target sequence is the arginine-rich sequence RnX(S/T)YY, where n is Ն2, X can be Arg, Ala, Val, Pro, or Ser, and Y can be any amino acid except an acidic residue (67)(68)(69). Therefore, p32 may regulate Us3 phosphorylation of UL31 and gB by binding to the phosphorylation sites in gB and UL31 to promote perinuclear fusion activity for HSV-1 de-envelopment.…”

Section: Discussionmentioning

confidence: 99%

Role of Host Cell p32 in Herpes Simplex Virus 1 De-Envelopment during Viral Nuclear Egress

Liu

Kato

Oyama

et al. 2015

J Virol

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To clarify the function(s) of the herpes simplex virus 1 (HSV-1) major virion structural protein UL47 (also designated VP13/14), we screened cells overexpressing UL47 for UL47-binding cellular proteins. Tandem affinity purification of transiently expressed UL47 coupled with mass spectrometry-based proteomics technology and subsequent analyses showed that UL47 interacted with cell protein p32 in HSV-1-infected cells. Unlike in mock-infected cells, p32 accumulated at the nuclear rim in HSV-1-infected cells, and this p32 recruitment to the nuclear rim required UL47. p32 formed a complex(es) with HSV-1 proteins UL31, UL34, Us3, UL47, and/or ICP22 in HSV-1-infected cells. All these HSV-1 proteins were previously reported to be important for HSV-1 nuclear egress, in which nucleocapsids bud through the inner nuclear membrane (primary envelopment) and the enveloped nucleocapsids then fuse with the outer nuclear membrane (de-envelopment). Like viral proteins UL31, UL34, Us3, and UL47, p32 was detected in primary enveloped virions. p32 knockdown reduced viral replication and induced membranous invaginations adjacent to the nuclear rim containing primary enveloped virions and aberrant localization of UL31 and UL34 in punctate structures at the nuclear rim. These effects of p32 knockdown were reduced in the absence of UL47. Therefore, the effects of p32 knockdown in HSV-1 nuclear egress were similar to those of the previously reported mutation(s) in HSV-1 regulatory proteins for HSV-1 de-envelopment during viral nuclear egress. Collectively, these results suggested that p32 regulated HSV-1 de-envelopment and replication in a UL47-dependent manner. IMPORTANCEIn this study, we have obtained data suggesting that (i) the HSV-1 major virion structural protein UL47 interacted with host cell protein p32 and mediated the recruitment of p32 to the nuclear rim in HSV-1-infected cells; (ii) p32 was a component of the HSV-1 nuclear egress complex (NEC), whose core components were UL31 and UL34; and (iii) p32 regulated HSV-1 de-envelopment during viral nuclear egress. It has been reported that p32 was a component of human cytomegalovirus NEC and was required for efficient disintegration of nuclear lamina, which has been thought to facilitate HSV-1 primary envelopment during viral nuclear egress. Thus, p32 appeared to be a core component of herpesvirus NECs, like UL31 and UL34 homologs in other herpesviruses, and to play multiple roles in herpesvirus nuclear egress. H erpesvirus nucleocapsids are too large to traverse the nuclear lamina or cross the inner (INM) and outer (ONM) nuclear membranes through nuclear pores. Therefore, herpesviruses appear to have evolved a unique nuclear egress mechanism in which progeny nucleocapsids assembled in the nucleus acquire primary envelopes by budding through the INM into the perinuclear space (primary envelopment), the space between the INM and ONM, and enveloped nucleocapsids then fuse with the ONM to release de-enveloped nucleocapsids into the cytoplasm (de-envelopment) (1, 2). A heterodim...

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“…In the late 1970s, the first reports speculating about the existence of viral kinases were published (40,206); it was only 10 years later that the first viral kinases were identified (115,117). Over the last few years, several new insights have been gained concerning the often pleiotropic functions of viral protein kinases.…”

mentioning

confidence: 99%

Viral Serine/Threonine Protein Kinases

Jacob

Broeke

Favoreel

2011

J Virol

109

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Phosphorylation represents one the most abundant and important posttranslational modifications of proteins, including viral proteins. Virus-encoded serine/threonine protein kinases appear to be a feature that is unique to large DNA viruses. Although the importance of these kinases for virus replication in cell culture is variable, they invariably play important roles in virus virulence. The current review provides an overview of the different viral serine/threonine protein kinases of several large DNA viruses and discusses their function, importance, and potential as antiviral drug targets.

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Viral protein kinases and protein phosphatases

Cited by 48 publications

References 219 publications

Phosphorylation of the Epstein-Barr Virus (EBV) DNA Polymerase Processivity Factor EA-D by the EBV-Encoded Protein Kinase and Effects of the l -Riboside Benzimidazole 1263W94

Phosphorylation of the Epstein-Barr Virus (EBV) DNA Polymerase Processivity Factor EA-D by the EBV-Encoded Protein Kinase and Effects of the l -Riboside Benzimidazole 1263W94

Role of Host Cell p32 in Herpes Simplex Virus 1 De-Envelopment during Viral Nuclear Egress

Viral Serine/Threonine Protein Kinases

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