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DC-SIGN and DC-SIGNR Interact with the Glycoprotein of Marburg Virus and the S Protein of Severe Acute Respiratory Syndrome Coronavirus

Andrea Marzi,^1,2, Thomas Gramberg,^1,2, Graham Simmons,^3, Peggy Möller,⁴ Andrew J. Rennekamp,³ Mandy Krumbiegel,^1,2 Martina Geier,^1,2 Jutta Eisemann,⁵ Nadine Turza,⁵ Bertrand Saunier,⁶ Alexander Steinkasserer,⁵ Stephan Becker,⁴ Paul Bates,³ Heike Hofmann,^1,2 and Stefan Pöhlmann^1,2*

Institute for Clinical and Molecular Virology,¹ Nikolaus-Fiebiger-Center,² Department of Dermatology, University of Erlangen-Nürnberg, Erlangen,⁵ Institute for Virology, Philipps-University Marburg, Marburg, Germany,⁴ Department of Microbiology, University of Pennsylvania, Philadelphia, Pennsylvania,³ Edison Biotechnology Institute and College of Osteopathic Medicine, Ohio University, Athens, Ohio⁶

Received 8 March 2004/ Accepted 24 June 2004

The lectins DC-SIGN and DC-SIGNR can augment viral infection; however, the range of pathogens interacting with these attachment factors is incompletely defined. Here we show that DC-SIGN and DC-SIGNR enhance infection mediated by the glycoprotein (GP) of Marburg virus (MARV) and the S protein of severe acute respiratory syndrome coronavirus and might promote viral dissemination. SIGNR1, a murine DC-SIGN homologue, also enhanced infection driven by MARV and Ebola virus GP and could be targeted to assess the role of attachment factors in filovirus infection in vivo.

A.M., T.G., and G.S. contributed equally to this work.

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