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J. Biol. Chem., Vol. 279, Issue 42, 43661-43666, October 15, 2004

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A Novel Sorting Signal for Intracellular Localization Is Present in the S Protein of a Porcine Coronavirus but Absent from Severe Acute Respiratory Syndrome-associated Coronavirus^*

Christel Schwegmann-Wessels, Marwan Al-Falah, David Escors¶, Zai Wang||, Gert Zimmer, Hongkui Deng||, Luis Enjuanes¶, Hassan Y. Naim, and Georg Herrler**

From the Institut für Virologie and Institut für Physiologische Chemie, Tierärztliche Hochschule Hannover, Bünteweg 17, D-30559 Hannover, Germany, ^¶Centro Nacional de Biotecnologia, Consejo Superior de Investigaciones Científicas, Department of Molecular and Cell Biology, Campus Universidad Autonoma, Cantoblanco, 28049 Madrid, Spain, and the ^||Department of Cell Biology and Genetics, College of Life Sciences, Peking University, Beijing 100871, China

Coronaviruses (CoV) mature by a budding process at intracellular membranes. Here we showed that the major surface protein S of a porcine CoV (transmissible gastroenteritis virus) is not transported to the cell surface but is retained intracellularly. Site-directed mutagenesis indicated that a tyrosine-dependent signal (YXXI) in the cytoplasmic tail is essential for intracellular localization of the S protein. Surface expression of mutant proteins was evident by immunofluorescence analysis and surface biotinylation. Intracellularly retained S proteins only contained endoglycosidase H-sensitive N-glycans, whereas mutant proteins that migrated to the plasma membrane acquired N-linked oligosaccharides of the complex type. Corresponding tyrosine residues are present in the cytoplasmic tails of the S proteins of other animal CoV but not in the tail portion of the S protein of severe acute respiratory syndrome (SARS)-CoV. Changing the SEPV tetrapeptide in the cytoplasmic tail to YEPI resulted in intracellular retention of the S protein of SARS-CoV. As the S proteins of CoV have receptor binding and fusion activities and are the main target of neutralizing antibodies, the differences in the transport behavior of the S proteins suggest different strategies in the virus host interactions between SARS-CoV and other coronaviruses.

Received for publication, June 28, 2004 , and in revised form, August 10, 2004.

^* This work was supported by a grant from Deutsche Forschungsgemeinschaft (SFB 621) (to G. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

^** To whom correspondence should be addressed: Institut für Virologie, Tierärztliche Hochschule Hannover, Bünteweg 17, D-30559 Hannover, Germany. Tel.: 49-511-953-8857; Fax: 49-511-953-8898; E-mail: Georg.Herrler{at}tiho-hannover.de.

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