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

被引：14

作者：

Horie, Y

Nakagomi, T

Oseto, M

Masamune, O

Nakagomi, O

机构：

[1] AKITA UNIV, SCH MED, DEPT MICROBIOL, AKITA 010, JAPAN

[2] DEPT INTERNAL MED 1, AKITA, JAPAN

[3] EHIME PREFECTURAL INST PUBL HLTH, MATSUYAMA, EHIME, JAPAN

来源：

ARCHIVES OF VIROLOGY | 1997年 / 142卷 / 09期

关键词：

D O I：

10.1007/s007050050204

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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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页码：1865 / 1872

页数：8

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