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Comparative Study
. 1997;142(9):1865-72.
doi: 10.1007/s007050050204.

Conserved structural features of nonstructural glycoprotein NSP4 between group A and group C rotaviruses

Y Horie  1 , T Nakagomi, M Oseto, O Masamune, O Nakagomi
Affiliations
Comparative Study

Conserved structural features of nonstructural glycoprotein NSP4 between group A and group C rotaviruses

Y Horie et al. Arch Virol. 1997.

Abstract

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.

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