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Journal of Virology, January 2000, p. 295-304, Vol. 74, No. 1
0022-538X/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Activation of a Cell Entry Pathway Common to Type C Mammalian Retroviruses by Soluble Envelope Fragments

Dimitri Lavillette,1,2 Alessia Ruggieri,1 Stephen J. Russell,3 and François-Loïc Cosset1,2,*

Laboratoire de Vectorologie Rétrovirale et Thérapie Génique, Unité de Virologie Humaine, INSERM U412, Ecole Normale Supérieure de Lyon, Lyon,1 and Centre de Génétique Moléculaire et Cellulaire, CNRS UMR5534, Université Claude-Bernard Lyon-1, Villeurbanne,2 France, and Molecular Medicine Program, Mayo Clinic, Rochester, Minnesota3

Received 2 July 1999/Accepted 20 September 1999

Mutations that negatively or positively affect the fusion properties of murine leukemia viruses (MLVs) have been found within all subdomains of their SU (surface) and TM (transmembrane) envelope units. Yet, the interrelations between these different regions of the envelope complex during the cell entry process are still elusive. Deletion of the histidine residue of the conserved PHQV motif at the amino terminus of the amphotropic or the ecotropic MLV SU resulted in the AdelH or the MOdelH fusion-defective mutant envelope, respectively. These delH mutant envelopes are incorporated on retroviral particles at normal densities and normally mediate virion binding to cells expressing the retroviral receptors. However, both their cell-cell and virus-cell fusogenicities were fully prevented at an early postbinding stage. We show here that the fusion defect of AdelH or MOdelH envelopes was also almost completely reverted by providing either soluble SU or a polypeptide encompassing the receptor-binding domain (RBD) to the target cells, provided that the integrity of the amino-terminal end of either polypeptide was preserved. Restoration of delH envelope fusogenicity was caused by activation of the target cells via specific interaction of the latter polypeptides with the retrovirus receptor rather than by their association with the delH envelope complexes. Moreover crossactivation of the target cells, leading to fusion activation of AdelH or MOdelH envelopes, was achieved by polypeptides containing various type C mammalian retrovirus RBDs, irrespective of the type of entry-defective glycoprotein that was used for infection. Our results indicate that although they recognize different receptors for binding to the cell surface, type C mammalian retroviruses use a common entry pathway which is activated by a conserved feature of their envelope glycoproteins.

* Corresponding author. Mailing address: LVRTG, INSERM U412, Ecole Normale Supérieure de Lyon, 46 Allée d'Italie, 69364 Lyon Cedex 07, France. Phone and fax: 33 472 72 87 32. E-mail: Francois-Loic.Cosset{at}ens-lyon.fr.

Journal of Virology, January 2000, p. 295-304, Vol. 74, No. 1
0022-538X/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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