3C-like proteinase
A Novel Mutation in Murine Hepatitis Virus nsp5, the Viral 3C-Like Proteinase, Causes Temperature-Sensitive Defects in Viral Growth and Protein Processing
... cysteine proteinase that is essential for virus polyprotein processing and ...The 3C-like proteinase activity of nsp5 was first experimentally confirmed in our laboratory (33) and, since the ...
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Characterization of a human coronavirus (strain 229E) 3C-like proteinase activity.
... the 3C proteinase of ...229E 3C-like proteinase domain as part of a b -galactosidase fusion protein in Escherichia coli and have shown that the expressed protein has proteolytic ...
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Characterization in vitro of an autocatalytic processing activity associated with the predicted 3C-like proteinase domain of the coronavirus avian infectious bronchitis virus.
... predicted 3C-like proteinase (3CLP) domain and several potential cleavage sites has been cloned into a T7 transcription ...IBV 3C-like proteinase, which exhibits characteristics ...
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Functional and Genetic Studies of the Substrate Specificity of Coronavirus Infectious Bronchitis Virus 3C-Like Proteinase
... (CoV) 3C-like proteinase (3CLpro), located in nonstructural protein 5 (nsp5), processes the replicase polyproteins 1a and 1ab (pp1a and pp1ab) at 11 specific sites to produce 12 mature nonstructural ...
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Biosynthesis, purification, and characterization of the human coronavirus 229E 3C-like proteinase.
... tions are occupied by Leu/Ile and Ser/Ala, respectively. The data we present above are consistent with a substrate “core” represented by the amino acid sequence Ile/Leu-Gln- Ala/Ser. However, at the present time, we do ...
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The 3C-Like Proteinase of an Invertebrate Nidovirus Links Coronavirus and Potyvirus Homologs
... Comparative sequence analysis revealed several putative functional domains in the GAV polyproteins, including heli- case and polymerase motifs, ordered similarly to the cognate domains in the viral polyproteins of other ...
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Processing of the Human Coronavirus 229E Replicase Polyproteins by the Virus-Encoded 3C-Like Proteinase: Identification of Proteolytic Products and Cleavage Sites Common to pp1a and pp1ab
... 1 Processing of the Human Coronavirus 229E Replicase Polyproteins by the Virus-Encoded 3C-Like Proteinase: Identification of Proteolytic Products and Cleavage Sites Common to pp1a and pp[r] ...
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Cinanserin Is an Inhibitor of the 3C-Like Proteinase of Severe Acute Respiratory Syndrome Coronavirus and Strongly Reduces Virus Replication In Vitro
... In contrast to purely experimental compounds, cinanserin (SQ 10,643) is a drug that has already undergone clinical eval- uation. It had been synthesized and characterized as a seroto- nin inhibitor by The Squibb ...
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Expression of Murine Coronavirus Recombinant Papain-Like Proteinase: Efficient Cleavage Is Dependent on the Lengths of both the Substrate and the Proteinase Polypeptides
... papain-like proteinase (PLP) domains, an X domain of unknown function adjacent to PLP-1, and a polio- virus 3C-like proteinase ...
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Identification and characterization of a serine-like proteinase of the murine coronavirus MHV-A59.
... the 3C proteinases of the picornaviruses ...putative 3C-like proteinase domain of MHV-A59, along with portions of the flanking hydrophobic ...active proteinase within the ...
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Identification of Mouse Hepatitis Virus Papain-Like Proteinase 2 Activity
... papain-like proteinase 1 (PLP1) and the poliovirus 3C-like proteinase (3CLpro), have been shown to process the replicase ...MHV proteinase domain, ...viral proteinase ...
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Identification of Active-Site Amino Acid Residues in the Chiba Virus 3C-Like Protease
... The 3C-like protease of the Chiba virus, a Norwalk-like virus, is one of the chymotrypsin-like ...active 3C-like protease would cleave 3BC into 3B (VPg) and 3C ...the ...
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Cleavage of Poly(A)-Binding Protein by Poliovirus 3C Proteinase Inhibits Viral Internal Ribosome Entry Site-Mediated Translation
... Viral IRES-mediated translation decreases late in infection when the RNA genome is replicated. Viral translation and RNA replication cannot occur simultaneously on the same template; in a situation where either scenario ...
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Broad-Spectrum Inhibitors against 3C-Like Proteases of Feline Coronaviruses and Feline Caliciviruses
... Viral 3C-like protease (3CLpro) is responsible for processing of the majority of cleavage sites; thus, it is essential in the replication of coronaviruses and ...
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Identification of the catalytic sites of a papain-like cysteine proteinase of murine coronavirus.
... Among the Cys and His residues within the predicted proteinase domain, Cys-1137 and His-1288 are the only two conserved among all the cellular and viral papain-like thiol proteinases, an[r] ...
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Genetic Screen for Monitoring Severe Acute Respiratory Syndrome Coronavirus 3C-Like Protease
... -Gal–SCoV 3C-like protease construct and the ...-Gal–SCoV 3C-like pro- tease construct and the ...-Gal–SCoV 3C-like pro- tease construct and the ...-Gal–SCoV 3C- ...
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Characterization of an Alphamesonivirus 3C-Like Protease Defines a Special Group of Nidovirus Main Proteases
... ronivirus 3C-like proteases employ a catalytic Cys-His dyad (19, ...nidovirus 3C-like proteases have a par- tially conserved substrate specificity, with Gln or Glu occupying the P1 position ...
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Characterization of a Torovirus Main Proteinase
... two proteinase domains were found: a cysteine pro- teinase within the N-terminal half of pp1a and a more C-termi- nally located serine proteinase ...
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Site-directed mutagenesis of proteinase 3C results in a poliovirus deficient in synthesis of viral RNA polymerase.
... A previous report of a poliovirus mutant containing an amino acid insertion in protein 2A demonstrated that a virus deficient in the synthesis of viral proteins still can produce wild-ty[r] ...
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Recombinant Cystatin-Like Thiol Proteinase Inhibitor (rCTPI) of Cicer arietinum (Chickpea): A potential source of Bio-pesticide.
... cysteine proteinase inhibitors (CPIs) or thiol proteinase inhibitors (TPIs) belonging to the superfamily of evolutionary, structurally and functionally related proteins involved in the inhibition of papain ...
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