Human rhinovirus 3C protease: a cysteine protease showing the trypsin(ogen)-like fold
نویسندگان
چکیده
منابع مشابه
Conservation of amino acids in human rhinovirus 3C protease correlates with broad-spectrum antiviral activity of rupintrivir, a novel human rhinovirus 3C protease inhibitor.
The picornavirus 3C protease is required for the majority of proteolytic cleavages that occur during the viral life cycle. Comparisons of published amino acid sequences from 6 human rhinoviruses (HRV) and 20 human enteroviruses (HEV) show considerable variability in the 3C protease-coding region but strict conservation of the catalytic triad residues. Rupintrivir (formerly AG7088) is an irrever...
متن کاملIn vitro resistance study of rupintrivir, a novel inhibitor of human rhinovirus 3C protease.
Rupintrivir (formerly AG7088) is an irreversible inhibitor of the human rhinovirus (HRV) 3C protease that has been demonstrated to have in vitro activity against all HRVs tested, consistent with its interaction with a strictly conserved subset of amino acids in the 3C protease. The potential for resistance was studied following in vitro serial passage of HRV serotypes 14, 2, 39, and Hanks in th...
متن کاملCleavage of small peptides in vitro by human rhinovirus 14 3C protease expressed in Escherichia coli.
The 3C region of human rhinovirus 14 was expressed in Escherichia coli. The microbially synthesized protease was functional, since the expressed precursor underwent autoproteolytic processing to generate mature molecules of the expected molecular weight and antigenicity. Mutation of the putative active-site Cys-146 residue to an alanine resulted in the synthesis of unprocessed precursor molecul...
متن کاملNovel triterpene sulfates from Fusarium compactum using a rhinovirus 3C protease inhibitor screen.
Two novel triterpene sulfates have been isolated from Fusarium compactum by bioactivity-directed fractionation using an assay which measures the inhibition of proteolytic activity of rhinovirus 3C protease on a fluorogenic peptide substrate. The compounds were purified by countercurrent and reverse phase chromatographies. NMR, MS, UV and IR studies revealed two triterpene sulfates, uncommon met...
متن کاملRhinovirus 3C protease precursors 3CD and 3CD' localize to the nuclei of infected cells.
Human rhinovirus (HRV) 3C protease (3Cpro) plays several important roles in the virus replication cycle. This enzyme cleaves the viral polyprotein at discrete sites to produce mature viral proteins and also inhibits cellular RNA transcription. It is not clear, however, whether the observed transcriptional shutoff activities are due to 3Cpro itself or to 3Cpro-containing precursors, and where 3C...
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ژورنال
عنوان ژورنال: Biochemistry and Molecular Biology Education
سال: 2001
ISSN: 1470-8175,1539-3429
DOI: 10.1111/j.1539-3429.2001.tb00111.x