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Journal of Virology, February 2000, p. 1985-1993, Vol. 74, No. 4
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Proteolytic Cleavage of the Fusion Protein but Not Membrane Fusion Is Required for Measles Virus-Induced Immunosuppression In Vitro

Armin Weidmann,1 Andrea Maisner,2 Wolfgang Garten,2 Marion Seufert,1 Volker ter Meulen,1 and Sibylle Schneider-Schaulies1,*

Institute for Virology and Immunobiology, University of Würzburg, D-97078 Würzburg,1 and Institute for Virology, University of Marburg, D-35011 Marburg,2 Germany

Received 16 August 1999/Accepted 22 November 1999

Immunosuppression induced by measles virus (MV) is associated with unresponsiveness of peripheral blood lymphocytes (PBL) to mitogenic stimulation ex vivo and in vitro. In mixed lymphocyte cultures and in an experimental animal model, the expression of the MV glycoproteins on the surface of UV-inactivated MV particles, MV-infected cells, or cells transfected to coexpress the MV fusion (F) and the hemagglutinin (H) proteins was found to be necessary and sufficient for this phenomenon. We now show that MV fusion-inhibitory peptides do not interfere with the induction of immunosuppression in vitro, indicating that MV F-H-mediated fusion is essentially not involved in this process. Proteolytic cleavage of MV F0 protein by cellular proteases, such as furin, into the F1-F2 subunits is, however, an absolute requirement, since (i) the inhibitory activity of MV-infected BJAB cells was significantly impaired in the presence of a furin-inhibitory peptide and (ii) cells expressing or viruses containing uncleaved F0 proteins revealed a strongly reduced inhibitory activity which was improved following trypsin treatment. The low inhibitory activity of effector structures containing mainly F0 proteins was not due to an impaired F0-H interaction, since both surface expression and cocapping efficiencies were similar to those found with the authentic MV F and H proteins. These results indicate that the fusogenic activity of the MV F-H complexes can be uncoupled from their immunosuppressive activity and that the immunosuppressive domains of these proteins are exposed only after proteolytic activation of the MV F0 protein.

* Corresponding author. Mailing address: Institute for Virology of the University of Würzburg, Versbacher Str. 7, D-97078 Würzburg, Germany. Phone: 49-931-201-3895. Fax: 49-931-201-3934. E-mail: s-s-s{at}vim.uni-wuerzburg.de.

Journal of Virology, February 2000, p. 1985-1993, Vol. 74, No. 4
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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