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Journal of Virology, September 2005, p. 11901-11913, Vol. 79, No. 18
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.18.11901-11913.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

The Carboxy-Terminal Sequence of the Pestivirus Glycoprotein E^rns Represents an Unusual Type of Membrane Anchor

Christiane Fetzer, Birke Andrea Tews, and Gregor Meyers^*

Institut für Immunologie, Friedrich-Loeffler-Institut, D-72001 Tübingen, Germany

Received 4 February 2005/ Accepted 17 June 2005

The E^rns protein is a structural glycoprotein of pestiviruses that lacks a typical membrane anchor sequence and is known to be secreted from the infected cell. However, major amounts of the protein are retained within the cell and attached to the virion by a so far unknown mechanism. Transient-expression studies with cDNA constructs showed that in a steady-state situation, 16% of the protein is found in the supernatant of the transfected cells while 84% appears as intracellular protein. We show here that E^rns represents a membrane-bound protein. Membrane binding occurs via the carboxy-terminal region of E^rns. By fusion of this sequence to the carboxy terminus of green fluorescent protein (GFP), the subcellular localization of the reporter protein switched from cytosolic to membrane bound. A core sequence of 11 amino acids necessary for membrane binding was elicited in truncation experiments with GFP constructs. However, this peptide is not sufficient to confer membrane anchoring but needs either upstream or downstream accessory sequences. Analyses with different extraction procedures showed that E^rns is neither easily stripped from the membrane, like a peripheral membrane protein, nor as tightly membrane bound as a transmembrane protein.

Present address: bioScreen European Veterinary Disease Management Center GmbH, D-48149 Münster, Germany.

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