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Journal of Virology, August 2005, p. 10467-10477, Vol. 79, No. 16
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.16.10467-10477.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

A Chimeric Respiratory Syncytial Virus Fusion Protein Functionally Replaces the F and HN Glycoproteins in Recombinant Sendai Virus

Gert Zimmer,1* Sascha Bossow,2 Larissa Kolesnikova,3 Matthias Hinz,1 Wolfgang J. Neubert,2 and Georg Herrler1

Institut für Virologie, Stiftung Tierärztliche Hochschule Hannover, Bünteweg 17, D-30559 Hannover,1 Max-Planck-Institut für Biochemie, Am Klopferspitz 18, D-82152 Martinsried,2 Institut für Virologie, Philipps-Universität, Robert-Koch-Straße 17, D-35037 Marburg, Germany3

Received 11 January 2005/ Accepted 4 May 2005

Entry of most paramyxoviruses is accomplished by separate attachment and fusion proteins that function in a cooperative manner. Because of this close interdependence, it was not possible with most paramyxoviruses to replace either of the two protagonists by envelope glycoproteins from related paramyxoviruses. By using reverse genetics of Sendai virus (SeV), we demonstrate that chimeric respiratory syncytial virus (RSV) fusion proteins containing either the cytoplasmic domain of the SeV fusion protein or in addition the transmembrane domain were efficiently incorporated into SeV particles provided the homotypic SeV-F was deleted. In the presence of SeV-F, the chimeric glycoproteins were incorporated with significantly lower efficiency, indicating that determinants in the SeV-F ectodomain exist that contribute to glycoprotein uptake. Recombinant SeV in which the homotypic fusion protein was replaced with chimeric RSV fusion protein replicated in a trypsin-independent manner and was neutralized by antibodies directed to RSV-F. However, replication of this virus also relied on the hemagglutinin-neuraminidase (HN) as pretreatment of cells with neuraminidase significantly reduced the infection rate. Finally, recombinant SeV was generated with chimeric RSV-F as the only envelope glycoprotein. This virus was not neutralized by antibodies to SeV and did not use sialic acids for attachment. It replicated more slowly than hybrid virus containing HN and produced lower virus titers. Thus, on the one hand RSV-F can mediate infection in an autonomous way while on the other hand it accepts support by a heterologous attachment protein.

* Corresponding author. Mailing address: Institut für Virologie, Tierärztliche Hochschule Hannover, Bünteweg 17, D-30559 Hannover, Germany. Phone: 49 511 953 8460. Fax: 49 511 953 8898. E-mail: Gert.Zimmer{at}tiho-hannover.de.

Journal of Virology, August 2005, p. 10467-10477, Vol. 79, No. 16
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.16.10467-10477.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.





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