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Journal of Biomedicine and Biotechnology
Volume 2010, Article ID 970491, 14 pages
http://dx.doi.org/10.1155/2010/970491
Research Article

Expression and Purification of Z Protein from Junín Virus

1Departamento de Ciencia y Tecnología, Universidad Nacional de Quilmes, LIGBCM, Roque Sáenz Peña 352, CP B1876BXD, Bernal, Buenos Aires, Argentina
2Department of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, MA 01003, USA
3Unité de Virologie Structurale, Pasteur Institut, 7524 París, France

Received 18 February 2010; Revised 14 April 2010; Accepted 21 April 2010

Academic Editor: Norbert K. Herzog

Copyright © 2010 S. E. Goñi et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Arenaviridae comprises 23 recognized virus species with a bipartite ssRNA genome and an ambisense coding strategy. The virions are enveloped and include nonequimolar amounts of each genomic RNA species, designated L and S, coding for four ORFs (N, GPC, L, and Z). The arenavirus Junín (JUNV) is the etiological agent of Argentine Hemorrhagic Fever, an acute disease with high mortality rate. It has been proposed that Z is the functional counterpart of the matrix proteins found in other negative-stranded enveloped RNA viruses. Here we report the optimized expression of a synthetic gene of Z protein, using three expression systems (two bacterial and a baculoviral one). One of these recombinant proteins was used to generate antibodies. A bioinformatic analysis was made where Z was subdivided into three domains. The data presented contributes methodologies for Z recombinant production and provides the basis for the development of new experiments to test its function.