title: Genetic selection of poliovirus 2Apro-binding peptides.
abstract: The yeast two-hybrid system has been used to identify mammalian clones that interact with poliovirus 2A proteinase (2Apro). Eight clones which encode previously unidentified human proteins were selected from a HeLa cell cDNA expression library. In addition, five clones encoding short peptides that interact with poliovirus 2Apro were also identified. The lengths of these peptides range from 6 to 30 amino acids, but all of them contain the Leu-X-Thr-Z motif (X represents any amino acid; Z represents a hydrophobic residue). This sequence is invariably located just at the carboxy terminus of each peptide. This approach raises the possibility of designing substrate analogue inhibitors of 2Apro. Thus, two nonhydrolyzable peptides containing the Leu-X-Thr-Z motif prevented cleavage of eukaryotic initiation factor 4G by poliovirus 2Apro in vitro. A more general method for identifying peptides with antiproteinase activity is discussed.
authors.affiliation: Centro de Biología Molecular "Severo Ochoa", Facultad de Ciencias, Universidad Autónoma de Madrid, Cantoblanco 28049, Madrid, Spain. IVENTOSO@TRASTO.CMB.UAM.ES
authors.forename: I
authors.initials: I
authors.lastname: Ventoso
authors.forename: A
authors.initials: A
authors.lastname: Barco
authors.forename: L
authors.initials: L
authors.lastname: Carrasco
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D015853:Cysteine Proteinase Inhibitors / Q000235:genetics* / Q000378:metabolism; D015723:Gene Library; D006367:HeLa Cells; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000235:genetics*; D012441:Saccharomyces cerevisiae / Q000235:genetics; D013329:Structure-Activity Relationship; D014764:Viral Proteins
chemical_list: D015853:Cysteine Proteinase Inhibitors; D010455:Peptides; D014764:Viral Proteins; D003546:Cysteine Endopeptidases; C057400:picornain 2A, Picornavirus