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Hepatitis C virus NS3 serine protease interacts with the serpin C1 inhibitor
Author(s) -
Drouet Christian,
Bouillet Laurence,
Csopaki Françoise,
Colomb Maurice G
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01194-1
Subject(s) - ns3 , serpin , masp1 , serine protease , protease , ns2 3 protease , chemistry , biochemistry , protease inhibitor (pharmacology) , proteolysis , cleavage (geology) , serine proteinase inhibitors , biology , virology , enzyme , virus , paleontology , fracture (geology) , antiretroviral therapy , viral load , gene
Both NS3 protein (1007–1657) and its protease moiety (NS3p, 1027–1207) were able to interact in vitro with C1 Inhibitor (C1Inh) to give a 95‐kDa M r C1Inh cleavage product similar to that obtained upon proteolysis by complement protease C1s. High‐ M r reaction products were also detected after incubation of C1Inh with NS3 but not with NS3p; they correspond to ester‐bonded complexes from their hydroxylamine lability. Similar reactivity of NS3 was observed upon incubation with α2‐antiplasmin. Serpin cleavage was prevented by treatment of NS3 with synthetic serine protease inhibitors. This interaction between viral NS3 and host serpins suggests that NS3 is likely to be controlled by infected cell protease inhibitors.