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M. I. Barría, A. González, J. Vera-Otarola, U. León, V. Vollrath, D. Marsac, O. Monasterio, T. Pérez-Acle, A. Soza and M. López-Lastra, “Analysis of Natural Variants of the he Patitis C Virus Internal Ribosome Entry Site Reveals That Primary Sequence Plays a Key Role in Cap-Independent Translation,” Nucleic Acids Research, Vol. 37, No. 3, 2009, pp. 957-971. doi:10.1093/nar/gkn1022

has been cited by the following article:

• TITLE: Characterization of Influenza H5N1 Nucleocapsid Protein for Potential Vaccine Design

  AUTHORS: Adam Buffone, Sophie Dionne, Mary Alice Hefford

  KEYWORDS: Quadrant Influenza; Therapeutic Vaccine; Nucleocapsid Protein; Physicochemical Characterization

  JOURNAL NAME: World Journal of Vaccines, Vol.2 No.3, August 3, 2012

  ABSTRACT: Avian influenza, subtype H5N1, causes occasional but serious infections in humans and efforts to produce vaccines against this strain continue. Current influenza vaccines are prophylactic and utilize the two major antigens, hemagglutinin and neuraminidase. Nucleocapsid protein (NP) is an attractive alternative antigen because it is highly conserved across all influenza strains, has been shown to increase the rate of viral clearance, and potential therapeutic vaccines would elicit cytotoxic T lymphocyte responses in an infected person. The NP antigen from H5N1 was characterized using a variety of physico-chemical methods to gain insights into both the biological and physical properties of the antigen which are important from a regulatory viewpoint when considering therapeutic vaccines. Results obtained to date show that NP is relatively unstable and indicate that the conformation of the H5N1 NP antigen is highly dependent upon purification procedure, buffer conditions, pH and the presence or absence of RNA. These factors will need to be clearly defined and taken into consideration when manufacturing and regulating NP vaccine preparations.