Coxsackievirus and adenovirus receptor amino-terminal immunoglobulin V-related domain binds adenovirus type 2 and fiber knob from adenovirus type 12

被引：80

作者：

Freimuth, P ^{[1
]}

Springer, K ^{[1
]}

Berard, C ^{[1
]}

Hainfeld, N ^{[1
]}

Bewley, M ^{[1
]}

Flanagan, J ^{[1
]}

机构：

[1] Brookhaven Natl Lab, Dept Biol, Upton, NY 11973 USA

来源：

JOURNAL OF VIROLOGY | 1999年 / 73卷 / 02期

关键词：

D O I：

10.1128/JVI.73.2.1392-1398.1999

中图分类号：

Q93 [微生物学];

学科分类号：

071005 [微生物学]; 100705 [微生物与生化药学];

摘要：

The extracellular region of the coxsackievirus and adenovirus receptor (CAR) is predicted to consist of two immunoglobulin (Ig)-related structural domains. We expressed the isolated CAR amino-terminal domain (D1) and a CAR fragment containing both extracellular Ig domains (D1/D2) in Escherichia coli. Both D1 and D1/D2 formed complexes in vitro with the recombinant knob domain of adenovirus type 12 (Ad12) fiber, and D1 inhibited adenovirus type 2 (Ad2) infection of HeLa cells. These results indicate that the adenovirus-binding activity of CAR is localized in the amino-terminal IgV-related domain and confirm our earlier observation that Ad2 and Ad12 bind to the same cellular receptor, Preliminary crystallization studies suggest that complexes of Ad12 knob bound to D1 will be suitable For structure determination.

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页码：1392 / 1398

页数：7

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