Cleavage site between VP1 and P2A of human rhinovirus is different in serotypes 2 and 14.
The viral capsid protein VP1 of human rhinovirus serotype 2 (HRV2) was cleaved with cyanogen bromide. The peptides thus obtained were separated on an HPLC butyl reversed phase column. Their positions on VP1 were determined by amino-terminal sequencing using the known nucleotide sequence of the genomic RNA of HRV2. The putative carboxy-terminal peptide was further cleaved with trypsin and the resulting fragments were separated on a C18 reversed phase column. Amino-terminus of sequencing of the C-terminal peptide revealed alanine as being the carboxy terminus of VP1 in HRV2. This indicates that the processing of the polyprotein is different in HRV2 from the processing previously reported for HRV14 and poliovirus.
Kowalski
H
H
Institut für Biochemie, Vienna, Austria.
Maurer-Fogy
I
I
Zorn
M
M
Mischak
H
H
Kuechler
E
E
Blaas
D
D
D000595:Amino Acid Sequence; D002213:Capsid / Q000378:metabolism*; D003488:Cyanogen Bromide; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D011498:Protein Precursors / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*; D012229:Rhinovirus / Q000378:metabolism*
D010446:Peptide Fragments; D011498:Protein Precursors; D011506:Proteins; D003488:Cyanogen Bromide