Cloning, expression and characterization of the proteinase from human herpesvirus 6.
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.
Tigue
N J
NJ
Department of Molecular and Medical Biosciences, University of Wales College of Cardiff, United Kingdom.
Matharu
P J
PJ
Roberts
N A
NA
Mills
J S
JS
Kay
J
J
Jupp
R
R
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
D011994:Recombinant Proteins; D010450:Endopeptidases