TY - JOUR
T1 - Hantavirus nucleocapsid protein interacts with the Fas-mediated apoptosis enhancer Daxx
AU - Li, Xiao Dong
AU - Mäkelä, Tomi P.
AU - Guo, Deyin
AU - Soliymani, Rabah
AU - Koistinen, Vesa
AU - Vapalahti, Olli
AU - Vaheri, Antti
AU - Lankinen, Hilkka
PY - 2002
Y1 - 2002
N2 - 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.
AB - 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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U2 - 10.1099/0022-1317-83-4-759
DO - 10.1099/0022-1317-83-4-759
M3 - Article
C2 - 11907324
AN - SCOPUS:0036208403
SN - 0022-1317
VL - 83
SP - 759
EP - 766
JO - Journal of General Virology
JF - Journal of General Virology
IS - 4
ER -