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J. Biol. Chem., Vol. 282, Issue 45, 32730-32741, November 9, 2007

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The Pestivirus Glycoprotein E^rns Is Anchored in Plane in the Membrane via an Amphipathic Helix^*

From the Institut für Immunologie, Friedrich-Loeffler-Institut, D-72001 Tübingen

E^rns is a structural glycoprotein of pestiviruses found to be attached to the virion and to membranes within infected cells via its COOH terminus, although it lacks a hydrophobic anchor sequence. The COOH-terminal sequence was hypothesized to fold into an amphipathic -helix. Alanine insertion scanning revealed that the ability of the E^rns COOH terminus to bind membranes is considerably reduced by the insertion of a single amino acid at a wide variety of positions. Mutations decreasing the hydrophobicity of the apolar face of the putative helix led to reduction of membrane association. Proteinase K protection assays showed that E^rns translated in vitro in the presence of microsomal membranes was protected, whereas a mutant with an artificial transmembrane region and a short cytosolic tag was shortened by the protease treatment. A tag fused to the COOH terminus of wild type E^rns was not accessible for antibodies within digitonin-permeabilized cells, but the variant with the tag located downstream of the artificial transmembrane region was detected under the same conditions. These results are in accordance with the model that the COOH-terminal membrane anchor of E^rns represents an amphipathic helix embedded in plane into the membrane. The integrity of the membrane anchor was found to be important for recovery of infectious virus.

Received for publication, August 15, 2007

^* This study was supported by a grant from Boehringer Ingelheim Vetmedica GmbH and by Deutsche Forschungsgemeinschaft Grant DFG Me/1367-4. 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.

¹ To whom correspondence should be addressed. Tel.: 49-7071-9670; Fax: 49-7071-967303; E-mail: gregor.meyers{at}fli.bund.de.

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				B. A. Tews, E.-M. Schurmann, and G. Meyers Mutation of Cysteine 171 of Pestivirus Erns RNase Prevents Homodimer Formation and Leads to Attenuation of Classical Swine Fever Virus J. Virol., May 15, 2009; 83(10): 4823 - 4834. [Abstract] [Full Text] [PDF]