Conserved structural features of nonstructural glycoprotein NSP4 between group A and group C rotaviruses |
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| Authors: | Y Horie T Nakagomi M Oseto O Masamune O Nakagomi |
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| Institution: | (1) The First Department of Internal Medicine, Akita, Japan, JP;(2) Department of Microbiology, Akita University School of Medicine, Akita, Japan, JP;(3) Ehime Prefectural Institute of Public Health, Matsuyama, Japan, JP |
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| Abstract: | Summary. 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.
Received January 10, 1997 Accepted April 24, 1997 |
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