Journal of General Virology

Hantavirus nucleocapsid protein interacts with the Fas-mediated apoptosis enhancer Daxx

Xiao-Dong Li,¹ Tomi P. Mäkelä,² Deyin Guo,³ Rabah Soliymani,¹ Vesa Koistinen,¹ Olli Vapalahti,¹ Antti Vaheri¹ and Hilkka Lankinen¹

Department of Virology¹ and Department of Pathology², Haartman Institute and HUCH Laboratory Diagnostics, and Institute of Biotechnology³, PO Box 21, Haartmaninkatu 3, FIN-00014 University of Helsinki, Finland

Hantaviruses cause two severe diseases, haemorrhagic fever with renal syndrome in Eurasia and hantavirus pulmonary syndrome in the Americas. To understand more about the molecular mechanisms that lead to these diseases, the associations of Puumala virus nucleocapsid protein (PUUV-N) with cellular proteins were studied by yeast two-hybrid screening. Daxx, known as an apoptosis enhancer, was identified from a HeLa cDNA library and its interaction with PUUV-N was confirmed by GST pull-down assay, co-immunoprecipitation and co-localization studies. Furthermore, domains of interaction were mapped to the carboxyl-terminal region of 142 amino acids in Daxx and the carboxyl-terminal 57 residues in PUUV-N, respectively. In pepscan assays, the binding sites of Daxx to PUUV-N were mapped further to two lysine-rich regions, of which one overlaps the sequence of the predicted nuclear localization signal of Daxx. These data suggest a direct link between host cell machinery and a hantavirus structural component.

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© 2002 SGM

This article is now available in the April 2002 print issue of JGV (vol. 83, 759–766). The complete issue of the journal may be seen in electronic form on JGV Online.