Poliovirus‐encoded proteinase 3C: a possible evolutionary link between cellular serine and cysteine proteinase families

  title={Poliovirus‐encoded proteinase 3C: a possible evolutionary link between cellular serine and cysteine proteinase families},
  author={Alexander E. Gorbalenya and Vladimir M. Blinov and Alexei P. Donchenko},
  journal={FEBS Letters},
Chimeric picornavirus polyproteins demonstrate a common 3C proteinase substrate specificity
Cross-species proteolytic processing was demonstrated by the 3C proteinases of human rhinovirus 14 and coxsackievirus B3 on poliovirus-specific polypeptide precursors, providing evidence for the existence of common conformational determinants necessary for 3C-mediated processing.
The picornaviral 3C proteinases: Cysteine nucleophiles in serine proteinase folds
  • B. Malcolm
  • Biology, Chemistry
    Protein science : a publication of the Protein Society
  • 1995
The recent determination of the structure of two of the 3C proteinases by X‐ray crystallography opens the door for the application of the latest advances in computer‐assisted identification and design of anti‐proteinase therapeutic/chemoprophylactic agents.
Viral cysteine proteinases
Dozens of novel cysteine proteinases have been identified in positive single-STRanded RNA viruses and, for the first time, in large double-stranded DNA viruses, indicating direct descendants of primordial proteolytic enzymes.
Identification of a trypsin-like serine proteinase domain encoded by ORF 1a of the coronavirus IBV.
Avian infectious bronchitis virus is the prototype species of the Coronaviridae, a family of enveloped viruses with large positive-stranded RNA genomes and three of these encode the major virion structural proteins spike, membrane, and nucleocapsid.


Human rhinovirus 2: complete nucleotide sequence and proteolytic processing signals in the capsid protein region.
cDNA clones representing the entire genome of human rhinovirus 2 have been obtained and used to determine the complete nucleotide sequence, thus defining the positions of three cleavage sites on the polyprotein.
The nucleotide and deduced amino acid sequences of the encephalomyocarditis viral polyprotein coding region.
Identification of the proteolytic cleavage sites showed that EMC viral protease, p22, has cleavage specificity forgln-gly or gln-ser sequences with adjacent proline residues, which includes both tyr-pro and glm-gly sequences.
Primary structure, gene organization and polypeptide expression of poliovirus RNA
The primary structure of the poliovirus genome has been determined and Twelve viral polypeptides have been mapped by amino acid sequence analysis and were found to be proteolytic cleavage products of the polyprotein, cleavages occurring predominantly at Gln-Gly pairs.
Similarity in gene organization and homology between proteins of animal picornaviruses and a plant comovirus suggest common ancestry of these virus families.
The amino acid sequences deduced from the nucleic acid sequences of several animal picornaviruses and cowpea mosaic virus and CPMV, a plant virus, were compared to conclude that the proteinases encoded by these viruses are probably cysteine proteinases, mechanistically related, but not homologous to papain.
Protease required for processing picornaviral coat protein resides in the viral replicase gene
Partial purification of the encephalomyocarditis protease synthesized in extracts from rabbit reticulocytes shows that the activity responsible for cleaving coat precursor protein cosediments with a
The complete nucleotide sequence of a common cold virus: human rhinovlrus 14
Comparison of the nucleotide sequence and the predicted amino acid sequence with those of the polioviruses reveals a surprising degree of homology which may allow recognition of regions of antigenic importance and prediction of the virus polyprotein cleavage sites.