2rlj

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Revision as of 11:50, 21 November 2007

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NMR Structure of Ebola fusion peptide in SDS micelles at pH 7

Overview

The fusion peptide EBO16 (GAAIGLAWIPYFG PAA) comprises the fusion domain, of an internal sequence located in the envelope fusion glycoprotein (GP2), of the Ebola virus. This region interacts with the cellular membrane of, the host and leads to membrane fusion. To gain insight into the mechanism, of the peptide- membrane interaction and fusion, insertion of the peptide, was modeled by experiments in which the tryptophan fluorescence and 1H-NMR, were monitored in the presence of sodium dodecyl sulfate micelles or in, the presence of detergent-resistant membrane fractions (DRMs). In the, presence of SDS micelles, EBO16 undergoes a random coil-helix transition, showing a tendency to self-associate. The three-dimensional structure, displays a (3)10-helix in the central part of molecule, similar to the, fusion peptides of many known membrane fusion proteins. Our results also, reveal that EBO16 can interact with DRMs, and strongly suggest that Trp 8, and Phe 12 are important for structure maintenance within the membrane, bilayer. Replacement of tryptophan 8 with alanine (W8A) resulted in, dramatic loss of helical structure proving the importance of the aromatic, ring in stabilizing the helix. Molecular dynamics studies of the, interaction between the peptide and the target membrane also corroborated, the crucial participation of these aromatic residues. The, aromatic-aromatic interaction may provide a mechanism for the free-energy, coupling between random coil-helical transition and membrane anchoring., Our data shed light on the structural "domains" of fusion peptides, and, provide a clue for the development of a drug that might block the early, steps of viral infection.

About this Structure

2RLJ is a Single protein structure of sequence from Zaire ebolavirus. Full crystallographic information is available from OCA.

Reference

Structure of the Ebola fusion peptide in a membrane-mimetic environment and the interaction with lipid rafts., Freitas MS, Gaspar LP, Lorenzoni M, Almeida FC, Tinoco LW, Almeida MS, Maia LF, Degreve L, Valente AP, Silva JL, J Biol Chem. 2007 Jun 1;. PMID:17545161

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