Enzymes of Human Herpesviruses

1992 ◽  
Vol 57 (8) ◽  
pp. 1577-1612 ◽  
Author(s):  
Pavel Kramata ◽  
Ivan Votruba
Keyword(s):  
Binding Protein ◽  
Human Herpesvirus ◽  
Dna Helicase ◽  
Point Of View ◽  
Uracil Dna Glycosylase ◽  
Replication Complex ◽  
Viral Genomes ◽  
Origin Binding Protein ◽  
Antiviral Chemotherapy ◽  
Human Herpesviruses

The properties of human herpesvirus-encoded enzymes are reviewed and the importance of sequence analysis of viral genomes as well as the experiments on characteristics of enzymes isolated from infected cell cultures are emphasized. The following enzymes are described in detail: DNA replication complex consisting of DNA polymerase, DNA helicase-primase, single-stranded DNA binding protein and origin binding protein, further thymidine kinase, ribonucleotide reductase, deoxyuridine triphosphatase as well as uracil-DNA-glycosylase, deoxyribonuclease and protein kinase. The importance of these enzymes from the point of view of antiviral chemotherapy is discussed.

scholarly journals Sequence Requirements for Interaction of Human Herpesvirus 7 Origin Binding Protein with the Origin of Lytic Replication

2001 ◽  
Vol 75 (8) ◽  
pp. 3925-3936 ◽  
Author(s):  
Laurie T. Krug ◽  
Naoki Inoue ◽  
Philip E. Pellett
Keyword(s):  
Dna Binding ◽  
Binding Protein ◽  
Human Herpesvirus ◽  
Binding Activity ◽  
Lytic Replication ◽  
Heteroduplex Analysis ◽  
Recognition Sequence ◽  
Mobility Shift ◽  
Dna Binding Activity ◽  
Origin Binding Protein

ABSTRACT As do human herpesvirus 6 variants A and B (HHV-6A and -6B), HHV-7 encodes a homolog of the alphaherpesvirus origin binding protein (OBP), which binds at sites in the origin of lytic replication (oriLyt) to initiate DNA replication. In this study, we sought to characterize the interaction of the HHV-7 OBP (OBPH7) with its cognate sites in the 600-bp HHV-7oriLyt. We expressed the carboxyl-terminal domain of OBPH7 and found that amino acids 484 to 787 of OBPH7 were sufficient for DNA binding activity by electrophoretic mobility shift analysis. OBPH7 has one high-affinity binding site (OBP-2) located on one flank of an AT-rich spacer element and a low-affinity site (OBP-1) on the other. This is in contrast to the HHV-6B OBP (OBPH6B), which binds with similar affinity to its two cognate OBP sites in the HHV-6BoriLyt. The minimal recognition element of the OBP-2 site was mapped to a 14-bp sequence. The OBPH7 consensus recognition sequence of the 9-bp core, BRTYCWCCT (where B is a T, G, or C; R is a G or A; Y is a T or C; and W is a T or A), overlaps with the OBPH6B consensus YGWYCWCCY and establishes YCWCC as the roseolovirus OBP core recognition sequence. Heteroduplex analysis suggests that OBPH7interacts along one face of the DNA helix, with the major groove, as do OBPH6B and herpes simplex virus type 1 OBP. Together, these results illustrate both conserved and divergent DNA binding properties between OBPH7 and OBPH6B.

Human herpesviruses and atherosclerosis. Modern point of view

2015 ◽  
pp. 54-62 ◽  
Author(s):  
Elizaveta Nikitskaya ◽  
◽  
Elena Maryukhnich ◽  
Polina Savvinova ◽  
Natalia Pinegina ◽  
...  
Keyword(s):  
Point Of View ◽  
Human Herpesviruses
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