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Journal of Virology, February 1999, p. 1392-1398, Vol. 73, No. 2
0022-538X/99/$00.00+0

Coxsackievirus and Adenovirus Receptor Amino-Terminal Immunoglobulin V-Related Domain Binds Adenovirus Type 2 and Fiber Knob from Adenovirus Type 12

Paul Freimuth,* Karen Springer, Chris Berard, Jim Hainfeld, Maria Bewley, and John Flanagan

Biology Department, Brookhaven National Laboratory, Upton, New York 11973

Received 17 June 1998/Accepted 6 November 1998

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.

* Corresponding author. Mailing address: Biology Department, Brookhaven National Laboratory, Upton, NY 11973. Phone: (516) 344-3350. Fax: (516) 344-3407. E-mail: freimuth{at}bnl.gov.

Journal of Virology, February 1999, p. 1392-1398, Vol. 73, No. 2
0022-538X/99/$00.00+0


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