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J. Biol. Chem., Vol. 280, Issue 33, 29899-29903, August 19, 2005

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The Nipah Virus Fusion Protein Is Cleaved within the Endosomal Compartment^*

Sandra Diederich, Markus Moll, Hans-Dieter Klenk, and Andrea Maisner

From the Institute of Virology, Philipps University of Marburg, 35037 Marburg, Germany

Nipah virus (NiV) is a recently emerged and highly pathogenic paramyxovirus that causes a systemic infection in animals and humans and can infect a wide range of cultured cells. Interestingly, the NiV fusion (F) protein has a single arginine at the cleavage site similar to paramyxoviruses that are activated by exogenous trypsin-like enzymes only present in specific cells and tissues and therefore only cause localized infections. We show here that NiV F activation is not mediated by an exogenous serum protease but by an endogenous ubiquitous cellular protease after endocytosis of the protein. In addition to endocytosis, acidification of the endosome is a prerequisite for F cleavage. These results show that activation of the NiV F protein depends on a type of proteolytic cleavage that is clearly different from what is known for other paramyxoviral and orthomyxoviral fusion proteins. To our knowledge, this is the first example of a viral class I fusion protein whose activation depends on clathrin-mediated constitutive endocytosis.

Received for publication, April 27, 2005 , and in revised form, June 16, 2005.

^* This work was supported by Grant MA 1886/5-2 from the Deutsche Forschungsgemeinschaft (to A. M.). 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.

Present address: Center for Infectious Medicine, Karolinska Institute, Stockholm, Sweden.

To whom correspondence should be addressed: Institute of Virology, Robert-Koch-Str. 17, 35037 Marburg, Germany. Tel.: 49-6421-2865146; Fax: 49-6421-2868962; E-mail: maisner{at}staff.uni-marburg.de.

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