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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Antiviral research

Conservation of HHV-6 DNA polymerase processivity factor sequence and predicted structure suggests it as a target for antiviral development

Team: Archived: Type II topoisomerases challenges
Team: Structural Microbiology
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Antiviral research - 16 Mar 2010

Bonnafous P, Verbelen M, Petrella S, Deback C, Gautheret-Dejean A, Boutolleau D, Naesens L, Agut H

Link to Pubmed [PMID] – 20298721

Antiviral Res. 2010 Jun;86(3):316-9

The replication of human herpesvirus-6 (HHV-6) DNA is catalyzed by the viral DNA polymerase pU38 and the processivity factor pU27 which stabilizes the enzyme on the DNA template. The genetic polymorphism of pU27 among 46 clinical strains of HHV-6 variant A or B and four strains resistant to antivirals was investigated. Overall, 28 amino acid changes (7.6%) and a two-amino acid deletion were identified among the 368 residues of pU27, when using the U1102 (variant A) sequence as the reference. Eleven amino acid changes (3.0%) specifically differentiated both variants. The median intravariant amino acid variability was 1.2% and 0.3% for A and B, respectively. Except for a single change, the pU27 sequence of multi-drug resistant HHV-6 strains was also conserved. Structural models of pU27 for variants A and B were derived from that of the human cytomegalovirus homologue pUL44, and showed either identical or very similar residues in the regions interacting with viral DNA polymerase and viral DNA molecule. As pU27 is both highly conserved and essential for viral replication, it might constitute an interesting target for antiviral chemotherapy.