CONSERVED STRUCTURAL FEATURES OF NONSTRUCTURAL GLYCOPROTEIN NSP4 BETWEEN GROUP-A AND GROUP-C ROTAVIRUSES

Authors
HORIE Y NAKAGOMI T OSETO M MASAMUNE O NAKAGOMI O
Citation
Y. Horie et al., CONSERVED STRUCTURAL FEATURES OF NONSTRUCTURAL GLYCOPROTEIN NSP4 BETWEEN GROUP-A AND GROUP-C ROTAVIRUSES, Archives of virology, 142(9), 1997, pp. 1865-1872
Citations number
28
Categorie Soggetti
Virology
Journal title
Archives of virology → ACNP
ISSN journal
03048608
Volume
142
Issue
9
Year of publication
1997
Pages
1865 - 1872
Database
ISI
SICI code
0304-8608(1997)142:9<1865:CSFONG>2.0.ZU;2-N
Abstract
The nonstructural glycoprotein NSP4 of group C human rotavirus strain Ehime 9301 was determined to be 150 amino acids in length and 96% iden tical with the NSP4 of another group C human rotavirus strain Bristol. Both NSP4 sequences were virtually unrelated to group A rotavirus NSP 4s. However, the structural features of group A and group C rotavirus NSP4s were similar with hydrophobic domains being in the amino terminu s and a coiled coil domain after the membrane-spanning domain, althoug h group C rotavirus NSP4 lacked one amino-terminal hydrophobic domain.