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Journal of Virology, October 2006, p. 9837-9849, Vol. 80, No. 19
0022-538X/06/$08.00+0     doi:10.1128/JVI.00736-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Inhibition of Hendra Virus Fusion

M. Porotto,1 L. Doctor,1 P. Carta,1 M. Fornabaio,2 O. Greengard,1,3 G. E. Kellogg,2 and A. Moscona1*

Departments of Pediatrics and of Microbiology and Immunology, Weill Medical College of Cornell University, New York, New York 10021,1 Department of Medicinal Chemistry and Institute for Structural Biology and Drug Discovery, Virginia Commonwealth University, Richmond, Virginia 23298-0540,2 Mount Sinai School of Medicine, New York, New York3

Received 11 April 2006/ Accepted 12 July 2006

Hendra virus (HeV) is a recently identified paramyxovirus that is fatal in humans and could be used as an agent of bioterrorism. The HeV receptor-binding protein (G) is required in order for the fusion protein (F) to mediate fusion, and analysis of the triggering/activation of HeV F by G should lead to strategies for interfering with this key step in viral entry. HeV F, once triggered by the receptor-bound G, by analogy with other paramyxovirus F proteins, undergoes multistep conformational changes leading to a six-helix bundle (6HB) structure that accomplishes fusion of the viral and cellular membranes. The ectodomain of paramyxovirus F proteins contains two conserved heptad repeat regions (HRN and HRC) near the fusion peptide and the transmembrane domains, respectively. Peptides derived from the HRN and HRC regions of F are proposed to inhibit fusion by preventing F, after the initial triggering step, from forming the 6HB structure that is required for fusion. HeV peptides have previously been found to be effective at inhibiting HeV fusion. However, we found that a human parainfluenza virus 3 F-peptide is more effective at inhibiting HeV fusion than the comparable HeV-derived peptide.

* Corresponding author. Mailing address: Department of Pediatrics, Weill Medical College of Cornell University, 515 E. 71st St., 6th Floor, New York, NY 10021. Phone: (212) 746-4523. Fax: (212) 746-8261. E-mail: anm2047{at}med.cornell.edu.

Journal of Virology, October 2006, p. 9837-9849, Vol. 80, No. 19
0022-538X/06/$08.00+0     doi:10.1128/JVI.00736-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Whitman, S. D., Smith, E. C., Dutch, R. E. (2009). Differential Rates of Protein Folding and Cellular Trafficking for the Hendra Virus F and G Proteins: Implications for F-G Complex Formation. J. Virol. 83: 8998-9001 [Abstract] [Full Text]  
  • Porotto, M., Yokoyama, C. C., Orefice, G., Kim, H.-S., Aljofan, M., Mungall, B. A., Moscona, A. (2009). Kinetic Dependence of Paramyxovirus Entry Inhibition. J. Virol. 83: 6947-6951 [Abstract] [Full Text]  
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  • Deffrasnes, C., Hamelin, M.-E., Prince, G. A., Boivin, G. (2008). Identification and Evaluation of a Highly Effective Fusion Inhibitor for Human Metapneumovirus. Antimicrob. Agents Chemother. 52: 279-287 [Abstract] [Full Text]  
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  • Porotto, M., Fornabaio, M., Kellogg, G. E., Moscona, A. (2007). A Second Receptor Binding Site on Human Parainfluenza Virus Type 3 Hemagglutinin-Neuraminidase Contributes to Activation of the Fusion Mechanism. J. Virol. 81: 3216-3228 [Abstract] [Full Text]  
  • Luque, L. E., Russell, C. J. (2007). Spring-Loaded Heptad Repeat Residues Regulate the Expression and Activation of Paramyxovirus Fusion Protein. J. Virol. 81: 3130-3141 [Abstract] [Full Text]  


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