Conserved structural features of nonstructural glycoprotein NSP4 between group A and group C rotaviruses.
The nonstructural glycoprotein NSP4 of group C human rotavirus strain Ehime 9301 was determined to be 150 amino acids in length and 96% identical with the NSP4 of another group C human rotavirus strain Bristol. Both NSP4 sequences were virtually unrelated to group A rotavirus NSP4s. However, the structural features of group A and group C rotavirus NSP4s were similar with hydrophobic domains being in the amino terminus and a coiled coil domain after the membrane-spanning domain, although group C rotavirus NSP4 lacked one amino-terminal hydrophobic domain.
Horie
Y
Y
Department of Microbiology, Akita University School of Medicine, Japan.
Nakagomi
T
T
Oseto
M
M
Masamune
O
O
Nakagomi
O
O
D000465:Algorithms; D000595:Amino Acid Sequence; D001483:Base Sequence; D004721:Endoplasmic Reticulum / Q000821:virology; D006023:Glycoproteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D006801:Humans; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D012401:Rotavirus / Q000737:chemistry* / Q000145:classification / Q000254:growth & development; D016415:Sequence Alignment; D014118:Toxins, Biological; D017361:Viral Nonstructural Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology
D006023:Glycoproteins; C081369:NS28 protein, rotavirus; D014118:Toxins, Biological; D017361:Viral Nonstructural Proteins