Cleavage specificity on synthetic peptide substrates of human rhinovirus 2 proteinase 2A
| Autor: | Friederike Fessl, Dieter Blaas, Ingrid Maurer-Fogy, G Schnorrenberg, Ernst Kuechler, A Zöphel, Horst Ahorn, Wolfgang Sommergruber, Tim Skern, Hans-Dieter Liebig |
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| Rok vydání: | 1992 |
| Předmět: |
Rhinovirus
Stereochemistry Proteolysis Molecular Sequence Data Peptide Sodium Chloride Biology Cleavage (embryo) medicine.disease_cause Biochemistry Substrate Specificity Structure-Activity Relationship Viral Proteins medicine Protease Inhibitors Amino Acid Sequence Cloning Molecular Threonine Molecular Biology Escherichia coli chemistry.chemical_classification Base Sequence medicine.diagnostic_test Cell Biology Hydrogen-Ion Concentration Recombinant Proteins Amino acid Cysteine Endopeptidases Kinetics Enzyme Oligodeoxyribonucleotides chemistry Viral replication Peptides |
| Zdroj: | Europe PubMed Central |
| ISSN: | 0021-9258 |
| DOI: | 10.1016/s0021-9258(18)41720-6 |
| Popis: | Proteinase 2A of human rhinovirus serotype 2 (HRV2 2A) was expressed in Escherichia coli and partially purified; the preparation was used to study various enzymatic parameters. Using a 16-amino acid peptide representing the native cleavage region of HRV2 2A, an apparent Km value of 5.4 x 10(-4) mol/liter was determined. A minimum of 9 amino acids (comprising residues P8 to P1') was necessary for cleavage to occur. Proteolysis of substituted peptides was highly tolerant toward changes at P1, P2', and P3' but an absolute requirement for glycine P1' and a high preference for threonine P2 was found. Furthermore, HRV2 2A only cleaved peptide substrates derived from other rhinovirus serotypes and poliovirus that possessed P2 Thr and P1' Gly. Thus, the sequence Thr-X-Gly may form the basis of the cellular cleavage site processed by rhinoviral 2As during viral replication. Studies with various inhibitors support the hypothesis that HRV2 2A belongs to a new class of cysteine proteinases. |
| Databáze: | OpenAIRE |
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