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Journal of Virology, March 2004, p. 2627-2631, Vol. 78, No. 5
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.5.2627-2631.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Binding of the 2F5 Monoclonal Antibody to Native and Fusion-Intermediate Forms of Human Immunodeficiency Virus Type 1 gp41: Implications for Fusion-Inducing Conformational Changes

Eve de Rosny,1,{dagger} Russell Vassell,1 Shibo Jiang,2 Renate Kunert,3 and Carol D. Weiss1*

Center for Biologics Evaluation and Research, U.S. Food and Drug Administration, Bethesda, Maryland,1 Lindsley F. Kimball Research Institute, New York Blood Center, New York, New York,2 Institute of Applied Microbiology, Universität für Bodenkultur, Vienna, Austria3

Received 7 August 2003/ Accepted 11 November 2003

We investigated how the broadly neutralizing monoclonal antibody 2F5 affects the human immunodeficiency virus type 1 envelope glycoprotein as it undergoes receptor-induced conformational changes and show that 2F5 binds both native and fusion-intermediate conformations, suggesting inhibition of a late step in virus entry. We also demonstrate conformational changes in the C heptad of gp41.

* Corresponding author. Mailing address: FDA/CBER HFM-466, Bldg. 29, Room 532, 8800 Rockville Pike, Bethesda, MD 20892-4555. Phone: (301) 402-3190. Fax: (301) 496-1810. E-mail: cdweiss{at}helix.nih.gov.

{dagger} Present address: Laboratoire des proteines membranaires, Institut de Biologie Structurale, F-38027 Grenoble Cedex 1, France.

Journal of Virology, March 2004, p. 2627-2631, Vol. 78, No. 5
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.5.2627-2631.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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