title: Cloning, expression and characterization of the proteinase from human herpesvirus 6.
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.
authors.affiliation: Department of Molecular and Medical Biosciences, University of Wales College of Cardiff, United Kingdom.
authors.forename: N J
authors.initials: NJ
authors.lastname: Tigue
authors.forename: P J
authors.initials: PJ
authors.lastname: Matharu
authors.forename: N A
authors.initials: NA
authors.lastname: Roberts
authors.forename: J S
authors.initials: JS
authors.lastname: Mills
authors.forename: J
authors.initials: J
authors.lastname: Kay
authors.forename: R
authors.initials: R
authors.lastname: Jupp
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D010450:Endopeptidases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D015654:Herpesvirus 6, Human / Q000201:enzymology*; D006801:Humans; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D011817:Rabbits; D011994:Recombinant Proteins / Q000378:metabolism
chemical_list: D011994:Recombinant Proteins; D010450:Endopeptidases