TY - JOUR
T1 - A central hydrophobic domain of the hepatitis C virus NS4A protein is necessary and sufficient for the activation of the NS3 protease
AU - Tomei, Licia
AU - Failla, Cristina
AU - Vitale, Rosa Letizia
AU - Bianchi, Elisabetta
AU - De Francesco, Raffaele
PY - 1996
Y1 - 1996
N2 - The processing at the NS3/4A, NS4A/4B, NS4B/5A and NS5A/5B junctions in the non-structural region of the hepatitis C virus (HCV) polyprotein is performed by a viral serine protease activity contained within the N-terminal 180 amino acids of the NS3 protein. Full protease activity is only achieved upon the interaction of a region at the N terminus of NS3 with the NS4A protein, this region is also involved in the modulation of the protease activity. Using the rabbit reticulocyte expression system, we have defined the minimal domain of NS4A that is necessary to increase the cleavage efficiency of NS3. A synthetic peptide containing the same region, NS4A amino acids 21 to 32, stimulates the proteolytic activity of NS3 at all the trans-cleavage sites.
AB - The processing at the NS3/4A, NS4A/4B, NS4B/5A and NS5A/5B junctions in the non-structural region of the hepatitis C virus (HCV) polyprotein is performed by a viral serine protease activity contained within the N-terminal 180 amino acids of the NS3 protein. Full protease activity is only achieved upon the interaction of a region at the N terminus of NS3 with the NS4A protein, this region is also involved in the modulation of the protease activity. Using the rabbit reticulocyte expression system, we have defined the minimal domain of NS4A that is necessary to increase the cleavage efficiency of NS3. A synthetic peptide containing the same region, NS4A amino acids 21 to 32, stimulates the proteolytic activity of NS3 at all the trans-cleavage sites.
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M3 - Article
C2 - 8609472
AN - SCOPUS:0029940111
VL - 77
SP - 1065
EP - 1070
JO - Journal of General Virology
JF - Journal of General Virology
SN - 0022-1317
IS - 5
ER -