Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M601796200 on April 4, 2006

J. Biol. Chem., Vol. 281, Issue 23, 15951-15958, June 9, 2006
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
281/23/15951    most recent
M601796200v1
Right arrow Submit a Letter to Editor
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Kuhn, J. H.
Right arrow Articles by Farzan, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kuhn, J. H.
Right arrow Articles by Farzan, M.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Conserved Receptor-binding Domains of Lake Victoria Marburgvirus and Zaire Ebolavirus Bind a Common Receptor*

Jens H. Kuhn{ddagger}§1, Sheli R. Radoshitzky{ddagger}, Alexander C. Guth{ddagger}, Kelly L. Warfield, Wenhui Li{ddagger}, Martin J. Vincent||, Jonathan S. Towner||, Stuart T. Nichol||, Sina Bavari, Hyeryun Choe**, M. Javad Aman, and Michael Farzan{ddagger}2

From the {ddagger}Department of Microbiology and Molecular Genetics, Harvard Medical School, New England Primate Research Center, Southborough, Massachusetts 01772, the §Department of Biology, Chemistry, Pharmacy, Freie Universität Berlin, 14195 Berlin, Germany, the United States Army Medical Research Institute of Infectious Diseases, Ft. Detrick, Frederick, Maryland 21702, the ||Special Pathogens Branch, National Center for Infectious Diseases, Centers for Disease Control and Prevention, Atlanta, Georgia 30222, and the **Children's Hospital, Department of Pediatrics, Harvard Medical School, Boston, Massachusetts 02115

The GP1,2 envelope glycoproteins (GP) of filoviruses (marburg- and ebolaviruses) mediate cell-surface attachment, membrane fusion, and entry into permissive cells. Here we show that a 151-amino acid fragment of the Lake Victoria marburgvirus GP1 subunit bound filovirus-permissive cell lines more efficiently than full-length GP1. An homologous 148-amino acid fragment of the Zaire ebolavirus GP1 subunit similarly bound the same cell lines more efficiently than a series of longer GP1 truncation variants. Neither the marburgvirus GP1 fragment nor that of ebolavirus bound a nonpermissive lymphocyte cell line. Both fragments specifically inhibited replication of infectious Zaire ebolavirus, as well as entry of retroviruses pseudotyped with either Lake Victoria marburgvirus or Zaire ebolavirus GP1,2. These studies identify the receptor-binding domains of both viruses, indicate that these viruses utilize a common receptor, and suggest that a single small molecule or vaccine can be developed to inhibit infection of all filoviruses.


Received for publication, February 24, 2006 , and in revised form, March 30, 2006.

* This work was supported in part by Grant F_X012_04_RD_B from the Defense Threat Reduction Agency. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

1 Recipient of Career Development Fellowship Grant AI057159 from the New England Regional Center of Excellence/Biodefense and Infectious Diseases, Boston, MA.

2 To whom correspondence should be addressed: Dept. of Microbiology and Molecular Genetics, Harvard Medical School, New England Primate Research Center, 1 Pine Hill Dr., Southborough, MA 01772-9102. Tel.: 508-624-8019; Fax: 508-786-3317; E-mail: farzan{at}hms.harvard.edu.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Antimicrob. Agents Chemother.Home page
D. L. Swenson, K. L. Warfield, T. K. Warren, C. Lovejoy, J. N. Hassinger, G. Ruthel, R. E. Blouch, H. M. Moulton, D. D. Weller, P. L. Iversen, et al.
Chemical Modifications of Antisense Morpholino Oligomers Enhance Their Efficacy against Ebola Virus Infection
Antimicrob. Agents Chemother., May 1, 2009; 53(5): 2089 - 2099.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
D. Dube, M. B. Brecher, S. E. Delos, S. C. Rose, E. W. Park, K. L. Schornberg, J. H. Kuhn, and J. M. White
The Primed Ebolavirus Glycoprotein (19-Kilodalton GP1,2): Sequence and Residues Critical for Host Cell Binding
J. Virol., April 1, 2009; 83(7): 2883 - 2891.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
D. Dube, K. L. Schornberg, T. S. Stantchev, M. I. Bonaparte, S. E. Delos, A. H. Bouton, C. C. Broder, and J. M. White
Cell Adhesion Promotes Ebola Virus Envelope Glycoprotein-Mediated Binding and Infection
J. Virol., July 15, 2008; 82(14): 7238 - 7242.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
R. L. Kaletsky, G. Simmons, and P. Bates
Proteolysis of the Ebola Virus Glycoproteins Enhances Virus Binding and Infectivity
J. Virol., December 15, 2007; 81(24): 13378 - 13384.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
M. A. Brindley, L. Hughes, A. Ruiz, P. B. McCray Jr., A. Sanchez, D. A. Sanders, and W. Maury
Ebola Virus Glycoprotein 1: Identification of Residues Important for Binding and Postbinding Events
J. Virol., July 15, 2007; 81(14): 7702 - 7709.
[Abstract] [Full Text] [PDF]


Home page
J. Virol.Home page
M. Shimojima, A. Takada, H. Ebihara, G. Neumann, K. Fujioka, T. Irimura, S. Jones, H. Feldmann, and Y. Kawaoka
Tyro3 family-mediated cell entry of ebola and marburg viruses.
J. Virol., October 1, 2006; 80(20): 10109 - 10116.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2006 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement