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Journal of Virology, April 2001, p. 3960-3964, Vol. 75, No. 8
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.8.3960-3964.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Direct In Vitro Binding of Full-Length Human Immunodeficiency Virus Type 1 Nef Protein to CD4 Cytoplasmic Domain

Andrea Preusser,1 Lars Briese,1 Andreas S. Baur,2 and Dieter Willbold1,*

Institut für Molekulare Biotechnologie, D-07745 Jena,1 and Dermatologische Klinik, Universität Erlangen/Nürnberg, D-91052 Erlangen,2 Germany

Received 9 October 2000/Accepted 17 January 2001

The Nef protein of the simian and human immunodeficiency viruses is known to directly bind and downregulate the CD4 receptor. Although the molecular mechanism is well understood, direct binding of Nef and CD4 is difficult to demonstrate and is believed to be of low affinity. Applying nuclear magnetic resonance and fluorescence spectroscopy, we biophysically reevaluated the CD4-Nef complex and found the dissociation constant to be in the submicromolar range. We conclude that additional, so far disregarded residues in the N terminus of Nef are important for interaction with CD4.

* Corresponding author. Mailing address: Institut für Molekulare Biotechnologie, Beutenbergstr. 11, 07745 Jena, Germany. Phone: 49 3641 656440. Fax: 49 3641 656444. E-mail: willbold{at}imb-jena.de.

Journal of Virology, April 2001, p. 3960-3964, Vol. 75, No. 8
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.8.3960-3964.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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