title: Human rhinovirus 2: complete nucleotide sequence and proteolytic processing signals in the capsid protein region.
abstract: cDNA clones representing the entire genome of human rhinovirus 2 have been obtained and used to determine the complete nucleotide sequence. The genome consists of 7102 nucleotides and possesses a long open reading frame of 6450 nucleotides; this reading frame is initiated 611 nucleotides from the 5' end and stops 42 nucleotides from the polyA tract. The N-terminal sequences of three of the viral capsid proteins have been elucidated, thus defining the positions of three cleavage sites on the polyprotein. The extensive amino acid sequence homology with poliovirus and human rhinovirus 14 enabled the other cleavage sites to be predicted. Cleavages in the 3' half of the molecule appear to take place predominantly at Gln-Gly pairs, whereas those in the 5' half (including the capsid proteins) are more heterogeneous.
authors.forename: T
authors.initials: T
authors.lastname: Skern
authors.forename: W
authors.initials: W
authors.lastname: Sommergruber
authors.forename: D
authors.initials: D
authors.lastname: Blaas
authors.forename: P
authors.initials: P
authors.lastname: Gruendler
authors.forename: F
authors.initials: F
authors.lastname: Fraundorfer
authors.forename: C
authors.initials: C
authors.lastname: Pieler
authors.forename: I
authors.initials: I
authors.lastname: Fogy
authors.forename: E
authors.initials: E
authors.lastname: Kuechler
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D002213:Capsid / Q000235:genetics*; D003001:Cloning, Molecular; D005814:Genes, Viral; D006801:Humans; D010447:Peptide Hydrolases / Q000378:metabolism; D011498:Protein Precursors / Q000235:genetics*; D011499:Protein Processing, Post-Translational; D012229:Rhinovirus / Q000235:genetics*; D013379:Substrate Specificity
chemical_list: D011498:Protein Precursors; D010447:Peptide Hydrolases