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. 1996 Jun;70(6):4136–4141. doi: 10.1128/jvi.70.6.4136-4141.1996

Cloning, expression and characterization of the proteinase from human herpesvirus 6.

N J Tigue 1, P J Matharu 1, N A Roberts 1, J S Mills 1, J Kay 1, R Jupp 1
PMCID: PMC190303  PMID: 8648756

Abstract

After the U53 gene encoding the proteinase from human herpesvirus 6 (HHV-6) was sequenced, it was expressed in Escherichia coli, and the activity of the purified, recombinant HHV-6 proteinase was characterized quantitatively by using synthetic peptide substrates mimicking the release and maturation cleavage sites in the polyprotein precursors of HHV-6, human cytomegalovirus (CMV), murine CMV, and Epstein-Barr virus. Despite sharing 40% identity with other betaherpesvirus proteinases such as human CMV proteinase, the one-chain HHV-6 enzyme was distinguished from these two-chain proteinases by the absence of an internal autocatalytic cleavage site.

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Selected References

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