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Journal of Virology, December 2006, p. 11960-11967, Vol. 80, No. 24
0022-538X/06/$08.00+0 doi:10.1128/JVI.01678-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Hermann Bultmann,2
Curtis R. Brandt,1,2 and
Stacey Schultz-Cherry1*
Departments of Medical Microbiology and Immunology,1 Ophthalmology and Visual Sciences, University of Wisconsin, Madison, Wisconsin 537062
Received 3 August 2006/ Accepted 12 September 2006
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, for entry blocker) 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 postinfection. 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 protein. This novel peptide has potential value as a reagent to study virus attachment and as a future therapeutic.
Published ahead of print on 27 September 2006.
Present address: CIIT Centers for Health Research, 6 Davis Drive, P.O. Box 12137, Research Triangle Park, NC 27709.
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