Inhibition of Influenza Virus Infection by a Novel Antiviral Peptide that Targets Viral Attachment to Cells

October 18, 2006 — Jeremy C. Jones, Elizabeth A. Turpin, Hermann Bultmann, Curtis R. Brandt, and Stacey Schultz-Cherry

Influenza A viruses continue to cause widespread morbidity and mortality. There is an added concern that the highly pathogenic H5N1 influenza A viruses, currently found throughout many parts of the world, represent a serious public health threat and may result in a pandemic. Intervention strategies to halt an influenza epidemic or pandemic are a high priority with an emphasis on vaccines and antiviral drugs. In these studies, we demonstrate that a 20-amino acid peptide (EB) derived from the signal sequence of fibroblast growth factor-4 exhibits broad-spectrum antiviral activity against influenza viruses including the H5N1 subtype in vitro. The EB peptide was protective in vivo even when administered post-infection. Mechanistically, the EB peptide inhibits the attachment to the cellular receptor preventing infection. Further studies demonstrated that the EB peptide specifically binds to the viral hemagglutinin (HA) protein. This novel peptide has potential value as a reagent to study virus attachment and as a future therapeutic.

Copyright © 2006 by the American Society for Microbiology. All rights reserved.

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Jeremy C. Jones, Elizabeth A. Turpin, Hermann Bultmann, Curtis R. Brandt, and Stacey Schultz-Cherry Departments of Medical Microbiology and Immunology and Ophthalmology and Visual Sciences, University of Wisconsin, Madison, WI 53706 Address correspondence to: slschul2@wisc.edu