The amino acid sequence determination of a granulin and polyhedrin from two baculoviruses infecting Agrotis segetum.
The amino acid sequence of Agrotis segetum Granulosis virus (AsGV) granulin and A. Segetum nuclear polyhedrosis virus (AsNPV) polyhedrin was determined by sequencing tryptic and chymotryptic peptides from reduced and carboxymethylated proteins and tryptic fragments of oxidized and maleylated granulin. The comparison of the established peptide structures with the primary structures of other occlusion body proteins from related baculoviruses was also used for the polypeptide chains' reconstruction. The polypeptide chains of AsGV granulin and AsNPV polyhedrin comprise 247 and 246 amino acid residues, respectively. The proteins possess a high percentage of homology in their primary structures (63%).
Kozlov
E A
EA
Institute of Molecular Biology and Genetics, Academy of Sciences of the Ukraine, Kiev.
Rodnin
N V
NV
Levitina
T L
TL
Gusak
N M
NM
Radomskij
N F
NF
Palchikovskaya
L J
LJ
D000595:Amino Acid Sequence; D000818:Animals; D016367:Baculoviridae / Q000737:chemistry*; D007181:Inclusion Bodies, Viral / Q000737:chemistry*; D008969:Molecular Sequence Data; D009036:Moths / Q000382:microbiology*; D000077183:Occlusion Body Matrix Proteins; D010446:Peptide Fragments / Q000737:chemistry; D012689:Sequence Homology, Nucleic Acid; D015678:Viral Structural Proteins
D000077183:Occlusion Body Matrix Proteins; D010446:Peptide Fragments; D015678:Viral Structural Proteins; C000625703:granulin protein, granulovirus; C009829:polyhedrin protein, Nucleopolyhedrovirus