Single-chain Recombinant Human Cytomegalovirus Protease
نویسندگان
چکیده
منابع مشابه
Activity of two-chain recombinant human cytomegalovirus protease.
The human cytomegalovirus UL80 protease was expressed in Escherichia coli and purified by metal-chelate chromatography using a histidine tag engineered at the amino terminus. Cleavage of the 30-kDa protease at an internal site, VEA/A144, resulted in the recovery of 16- plus 14-kDa two-chain protease. The amino-terminal 16-kDa chain and the carboxyl-terminal 14-kDa chain remained associated as a...
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The protease domain of the murine cytomegalovirus (MCMV) M80 open reading frame was expressed in and purified from Escherichia coli. The recombinant enzyme was recovered as a mixture of active one- and two-chain forms. The two-chain enzyme was formed by internal cleavage of the one-chain enzyme at the I site. Activity measurements showed that MCMV protease cleaves R- and M-site peptide mimics w...
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OBJECTIVE To study the passive immunization with human monoclonal antibodies as for prophylaxis of human cytomegalovirus (HCMV) infection. METHODS Fab monoclonal antibodies to HCMV were recovered by repertoire cloning of mRNA from a HCMV infected individual. Antigen binding specificity, CDR sequence of V(H) and V(L) and neutralizing activity on HCMV AD169 stain were analyzed in vitro. The lig...
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conclusions gp55 of human cmv is considered as an important candidate for immunotherapy. in this study, we selected three specific clones against gp55. the scfvs reacted only with the corresponding peptide in a positive elisa. the scfv2 with 68.8% neutralizing effect showed the potential to be considered for prophylaxis and treatment of cmv infections, especially in solid organ transplant recip...
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Efficient proteolytic processing of essential junctions of the hepatitis C virus (HCV) polyprotein requires a heterodimeric complex of the NS3 bifunctional protease/helicase and the NS4A accessory protein. A single-chain recombinant form of the protease has been constructed in which NS4A residues 21-32 (GSVVIVGRIILS) were fused in frame to the amino terminus of the NS3 protease domain (residues...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1995
ISSN: 0021-9258
DOI: 10.1074/jbc.270.40.23634