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Journal of Virology, June 2002, p. 6382-6386, Vol. 76, No. 12
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.12.6382-6386.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Fatty Acid Modification of the Coxsackievirus and Adenovirus Receptor

Wouter van't Hof* and Ronald G. Crystal

Institute of Genetic Medicine, Weill Medical College of Cornell University, New York, New York

Received 13 December 2001/ Accepted 18 March 2002

Membrane-proximal cysteines 259 and 260 in the cytoplasmic tail of the coxsackievirus and adenovirus receptor (CAR) are known to be essential for the tumor suppression activity of CAR. We demonstrate that these residues provide an S-acylation motif for modification of CAR with the fatty acid palmitate. Substitution of alanine for cysteines 259 and 260 results in the additional localization of CAR in perinuclear compartments with no effect on the efficiency of adenovirus infection. The results indicate that palmitylation is important for stable plasma membrane expression and biological activity of CAR but is not critical for adenovirus receptor performance.

* Corresponding author. Mailing address: Institute of Genetic Medicine, Weill Medical College of Cornell University, 520 E. 70th St., Starr 505, New York, NY 10021. Phone: (212) 746-2258. Fax: (212) 746-8383. E-mail: geneticmedicine{at}med.cornell.edu.

Journal of Virology, June 2002, p. 6382-6386, Vol. 76, No. 12
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.12.6382-6386.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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