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J. Biol. Chem., Vol. 281, Issue 39, 29278-29286, September 29, 2006

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Structure of a Membrane-binding Domain from a Non-enveloped Animal Virus

INSIGHTS INTO THE MECHANISM OF MEMBRANE PERMEABILITY AND CELLULAR ENTRY^*

Lenize F. Maia, Márcia R. Soares, Ana P. Valente, Fabio C. L. Almeida, Andréa C. Oliveira, Andre M. O. Gomes, Monica S. Freitas, Anette Schneemann, John E. Johnson, and Jerson L. Silva¹

From the Programa de Biologia Estrutrural, Instituto de Bioquímica Médica and Centro Nacional de Ressonância Magnética Nuclear Jiri Jonas, Universidade Federal do Rio de Janeiro, 21941-590 Rio de Janeiro, RJ, Brazil, and the Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037

The ₁-peptide is a 21-residue lipid-binding domain from the non-enveloped Flock House virus (FHV). Unlike enveloped viruses, the entry of non-enveloped viruses into cells is believed to occur without membrane fusion. In this study, we performed NMR experiments to establish the solution structure of a membrane-binding peptide from a small non-enveloped icosahedral virus. The three-dimensional structure of the FHV ₁-domain was determined at pH 6.5 and 4.0 in a hydrophobic environment. The secondary and tertiary structures were evaluated in the context of the capacity of the peptide for permeabilizing membrane vesicles of different lipid composition, as measured by fluorescence assays. At both pH values, the peptide has a kinked structure, similar to the fusion domain from the enveloped viruses. The secondary structure was similar in three different hydrophobic environments as follows: water/trifluoroethanol, SDS, and membrane vesicles of different compositions. The ability of the peptide to induce vesicle leakage was highly dependent on the membrane composition. Although the -peptide shares some structural properties to fusion domains of enveloped viruses, it did not induce membrane fusion. Our results suggest that small protein components such as the -peptide in nodaviruses (such as FHV) and VP4 in picornaviruses have a crucial role in conducting nucleic acids through cellular membranes and that their structures resemble the fusion domains of membrane proteins from enveloped viruses.

Received for publication, May 16, 2006 , and in revised form, July 19, 2006.

^* This work was supported by grants from Conselho Nacional de Desenvolvimento Científico e Tecnológico, Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro, Millennium Institute for Structural Biology in Biomedicine and Biotechnology (Conselho Nacional de Desenvolvimento Científico e Tecnológico Millennium Program), Rede Nacional de Biologia Molecular Estrutural, Coordenação de Aperfeiçoamento de Pessoal de Nível Superior of Brazil, and by an international grant from the International Centre for Genetic Engineering and Biotechnology (to J. L. S.). 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.

The on-line version of this article (available at http://www.jbc.org) contains Figs. S1-S9.

¹ To whom correspondence should be addressed. E-mail: jerson{at}bioqmed.ufrj.br.

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