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

Xiao Dong Li, Tomi P. Mäkelä, Deyin Guo, Rabah Soliymani, Vesa Koistinen, Olli Vapalahti, Antti Vaheri, Hilkka Lankinen

Research output: Contribution to journalArticle

60 Citations (Scopus)

Abstract

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.

Original languageEnglish (US)
Pages (from-to)759-766
Number of pages8
JournalJournal of General Virology
Volume83
Issue number4
StatePublished - 2002

Fingerprint

Hantavirus
Nucleocapsid Proteins
Apoptosis
Hantavirus Pulmonary Syndrome
Hemorrhagic Fever with Renal Syndrome
Nuclear Localization Signals
Gene Library
Immunoprecipitation
Lysine
Yeasts
Binding Sites
Amino Acids
Puumala virus nucleocapsid protein
Proteins

ASJC Scopus subject areas

  • Virology
  • Immunology

Cite this

Li, X. D., Mäkelä, T. P., Guo, D., Soliymani, R., Koistinen, V., Vapalahti, O., ... Lankinen, H. (2002). Hantavirus nucleocapsid protein interacts with the Fas-mediated apoptosis enhancer Daxx. Journal of General Virology, 83(4), 759-766.

Hantavirus nucleocapsid protein interacts with the Fas-mediated apoptosis enhancer Daxx. / Li, Xiao Dong; Mäkelä, Tomi P.; Guo, Deyin; Soliymani, Rabah; Koistinen, Vesa; Vapalahti, Olli; Vaheri, Antti; Lankinen, Hilkka.

In: Journal of General Virology, Vol. 83, No. 4, 2002, p. 759-766.

Research output: Contribution to journalArticle

Li, XD, Mäkelä, TP, Guo, D, Soliymani, R, Koistinen, V, Vapalahti, O, Vaheri, A & Lankinen, H 2002, 'Hantavirus nucleocapsid protein interacts with the Fas-mediated apoptosis enhancer Daxx', Journal of General Virology, vol. 83, no. 4, pp. 759-766.
Li XD, Mäkelä TP, Guo D, Soliymani R, Koistinen V, Vapalahti O et al. Hantavirus nucleocapsid protein interacts with the Fas-mediated apoptosis enhancer Daxx. Journal of General Virology. 2002;83(4):759-766.
Li, Xiao Dong ; Mäkelä, Tomi P. ; Guo, Deyin ; Soliymani, Rabah ; Koistinen, Vesa ; Vapalahti, Olli ; Vaheri, Antti ; Lankinen, Hilkka. / Hantavirus nucleocapsid protein interacts with the Fas-mediated apoptosis enhancer Daxx. In: Journal of General Virology. 2002 ; Vol. 83, No. 4. pp. 759-766.
@article{3457030a12d1479b91853b73ae909506,
title = "Hantavirus nucleocapsid protein interacts with the Fas-mediated apoptosis enhancer Daxx",
abstract = "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.",
author = "Li, {Xiao Dong} and M{\"a}kel{\"a}, {Tomi P.} and Deyin Guo and Rabah Soliymani and Vesa Koistinen and Olli Vapalahti and Antti Vaheri and Hilkka Lankinen",
year = "2002",
language = "English (US)",
volume = "83",
pages = "759--766",
journal = "Journal of General Virology",
issn = "0022-1317",
publisher = "Society for General Microbiology",
number = "4",

}

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.

UR - http://www.scopus.com/inward/record.url?scp=0036208403&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036208403&partnerID=8YFLogxK

M3 - Article

VL - 83

SP - 759

EP - 766

JO - Journal of General Virology

JF - Journal of General Virology

SN - 0022-1317

IS - 4

ER -