Viral Aspects of Protein Phosphorylation

Herpes simplex virus type 2 (HSV-2) gene US3 has been shown to encode a serine-threonine protein kinase. In this study, we have tried to identify target proteins of the US3 protein kinase using a US3 lacZ insertion mutant of HSV-2. When permeabilized cells were labelled with [~-32p]ATP under the optimum conditions for the US3 enzyme, the most striking difference between wild-type HSV-2 strain 186-and mutant-infected cells was observed in the phosphorylation of proteins ranging in M r values from 14K to 22K. Studies of in vitro phosphorylation with purified virions and with cells infected with a US9-defective HSV-1 mutant suggested that a tegment phosphoprotein encoded by the US9 gene may be a target of HSV-2 US3 protein kinase.

supporting

confidence: 49%

Identification of a target protein of US3 protein kinase of herpes simplex virus type 2

Daikoku

Kurachi²,

Tsurumi³

et al. 1994

“…As viruses co-opt many cellular processes, it is natural to assume that the phosphorylation state of viral and cellular proteins can impinge on the viral life cycle. Thus, protein kinases and protein phosphatases may play a general role during viral infection for many viruses (reviewed in Leader & Katan, 1988).…”

Section: Introductionmentioning

confidence: 99%

The pk-1 Gene of Autographa Californica Multinucleocapsid Nuclear Polyhedrosis Virus Encodes a Protein Kinase

Reilly

Guarino

1994

Open reading frame (ORF) 9 of the EcoRI I fragment of the baculovirus Autographa californica multinucleocapsid nuclear polyhedrosis virus (AcMNPV) genome encodes a protein, PK-1, which has strong similarity to serine-threonine protein kinases. The published sequence of the pk-1 gene contains an error that, when corrected, extends the ORF by 228 nucleotides. Transcription of pk-1 was first detectable by primer extension at 12 h post-infection, accumulating to high levels during the very late phase of infection. PK-1 produced in rabbit reticulocyte lysates was able to phosphorylate histone H1. Together, our results suggest that ORF 9 encodes a protein kinase that is expressed during the beginning of the late and throughout the very late phases of AcMNPV infection.

“…Inspection of the dendrogram (Fig. 2b) shows that the MDV PK does not appear to share a common evolutionary pathway with the proto-oncogenes c-src (Takeya & Hanafusa, 1983) or c-mos (Watson et al, 1982a) but it is of interest that the kinases mapping in Us of the herpesviruses form a cluster with the cellular kinases cdc2 (Lee & Nurse, 1987), ribo-S6 kinase (Jones et aL, 1988) and yeast kin (Ohno et al, 1987) some role in controlling cell division (Leader & Katan, 1988;Peter et al, 1990). The amino acid similarities between the catalytic regions of MDV PK and those of HSV, VZV and PRV kinases using the GAP program (UWGCG) were estimated to be 60, 64 and 63~, respectively.…”

Section: Resultsmentioning

confidence: 99%

“…In particular, we focus on the MDV homologues of protein kinase (HSV US3) and the glycoproteins gD (HSV US6) and gI (HSV US7). In view of the role of phosphorylation in regulating the function of proteins and of the role of protein kinases in cell transformation (Leader & Katan, 1988), we were interested in determining the relationship between MDV protein kinase (MDV PK) and other kinases including the proto-oncogenes. Of the genes mapping in the Us region of alphaherpesviruses, gD has been shown to be essential for infectivity of HSV (Fuller & Spear, 1987) and to be an effective immunogen against acute and latent HSV infection (Cremer et al, 1985;Blacklaws & Nash, 1990).…”

Section: Introductionmentioning

confidence: 99%

Properties and evolutionary relationships of the Marek's disease virus homologues of protein kinase, glycoprotein D and glycoprotein I of herpes simplex virus

Ross¹,

Binns²

1991

The deduced amino acid sequences of the open reading frames (ORFs) mapping in the short unique segment (Us) of Marek's disease virus (MDV) reported in the accompanying paper have been analysed using computer programs to determine their relationships to herpesvirus proteins. Analysis of the catalytic domains of protein kinases showed that the MDV kinase (MDV PK) was closely related to the alphaherpesvirus protein kinase mapping in Us. The results also showed that the MDV PK was more closely related to the cellular kinases that control cell division than to the protooncogenes c-src and c-mos and it was predicted that the MDV PK would phosphorylate serine/threonine. The MDV homologue of herpes simplex virus (HSV) glycoprotein D (gD) contained several residues that were conserved in mammalian herpesviruses. In particular, six cysteines were perfectly aligned in all the gDs and there were numerous conservative substitutions.Although only approximately 65% of the MDV homologue of glycoprotein I (gI) of HSV has been sequenced, it was clear that a significant number of amino acid residues including four cysteines were conserved in the gI homologues of MDV and mammalian herpesviruses. Further analysis suggested that MDV gD was more closely related to the gDs of pseudorabies virus (PRV) and equine herpesvirus 1 than to the gD of HSV-1 and HSV-2. It was noted that HSV-2 glycoprotein G (gG), PRV gX and MDV gD were related and that MDV ORF4 was related to MDV gD and probably to HSV-1 gG. The results have shown a clear relationship between the genes of MDV and their counterparts in mammalian alphaherpesviruses and are consistent with the idea that MDV glycoprotein genes in Us might have arisen by a process ofgene duplication and independent evolution.