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Fold recognition insights into function of herpes ICP4 protein

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Wyrwicz L. S., Rychlewski L.

Acta Biochimica Polonica

2007

vol. 54

issue 3

551-559

ICP4 is an important factor regulating the life cycle of HSV1. This conserved protein has several molecular functions, including activation of expression of viral late gene transcripts and inhibition of immediate early genes. Although ICP4 and its Alphaherpesvirinae homologs (eg.: IE62 of VZV) have been subjects of various molecular studies, a complete view of their molecular function is lacking. Here we present the results of fold recognition and molecular modelling of ICP4 functional domains. The performed state-of-the-art bioinformatic fold recognition analysis identified a dual helix-turn-helix motif as a binding module of repressor activities (so called region 2 domain). The mapping of distant homology identified that a segment responsible for activation of late gene promoters (region 4) exhibits folding of uracil DNA glycosylase (UDG), but seems to be a non-functional homolog of UDG. Potential implications of the results are discussed.

Homologues of HSV-1 nuclear egress factor UL34 are potential phosphoinositide-binding proteins

100%

Wyrwicz L. S., Koczyk G., Rychlewski L.

Acta Biochimica Polonica

2008

vol. 55

issue 1

207-213

During the herpesvirus replication cycle, viral transcription, DNA replication, formation of capsids and DNA packaging occur in the nucleus. The subsequent nuclear egress of newly synthesized nucleocapsids is performed by budding of the inner leaflet of the nuclear membrane, which creates the primary envelope. Although products of two genes conserved throughout the Herpesviridae family (HSV-1 UL34 and UL31) have previously been shown to be involved in the execution of this process, the molecular basis of their activity is not clear. Here we present results of protein structure prediction for the conserved domain of UL34. The applied methodology suggests that this protein adopts a pleckstrin homology (PH) fold to perform its function. A detailed inspection of the ligand binding site strongly supports the hypothesis that UL34 orthologs can recognize phosphoinositides. Since previous works suggest that alterations of UL34 gene product result in a drastic impairment of primary envelopment of HSV-1 and trapping of capsids in the nucleus, the presented data may lead to the development of novel anti-herpetic therapeutic strategies where analogs of phosphoinositides are administered.

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2 Acta Biochimica Polonica

1 2008

1 2007

2 Rychlewski L.

2 Wyrwicz L. S.

1 Koczyk G.

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Fold recognition insights into function of herpes ICP4 protein

Homologues of HSV-1 nuclear egress factor UL34 are potential phosphoinositide-binding proteins