The "SARS-unique domain" (SUD) of SARS coronavirus is an oligo(G)-binding protein

Jinzhi Tan; Yuri Kusov; Doris Mutschall; Stefanie Tech; Krishna Nagarajan; Rolf Hilgenfeld; Christian L. Schmidt

doi:10.1016/j.bbrc.2007.10.081

The "SARS-unique domain" (SUD) of SARS coronavirus is an oligo(G)-binding protein

Jinzhi Tan, Yuri Kusov, Doris Mutschall, Stefanie Tech, Krishna Nagarajan, Rolf Hilgenfeld^*, Christian L. Schmidt

^*Corresponding author for this work

45 Citations (Scopus)

Abstract

Caused by a new coronavirus, severe acute respiratory syndrome (SARS) is a highly contagious disease associated with significant fatality that emerged in 2003. The molecular cause of the unusually high human pathogenicity of the SARS coronavirus (SARS-CoV) is still unknown. In an effort to characterize molecular components of the virus that are absent in other coronaviruses, all of which are considerably less pathogenic for humans, we recombinantly produced the SARS-unique domain (SUD) within non-structural protein 3 (Nsp3) of SARS-CoV and characterized its nucleic-acid binding properties. Zone-interference gel electrophoresis and electrophoretic mobility shift assays revealed a specific affinity of SUD for oligo(G)-strings. A few such segments are present in the SARS-CoV genome, but also in mRNAs of host proteins involved in the regulation of signaling pathways. A putative role of SUD in virus-induced apoptosis or survival of host cells is discussed.

Original language	English
Journal	Biochemical and Biophysical Research Communications
Volume	364
Issue number	4
Pages (from-to)	877-882
Number of pages	6
ISSN	0006-291X
DOIs	https://doi.org/10.1016/j.bbrc.2007.10.081
Publication status	Published - 28.12.2007

Funding

This work was supported by the Sino-European Project on SARS Diagnostics and Antivirals (SEPSDA) of the European Commission (contract number SP22-CT-2004-003831), the Sino-German Center for Promotion of Research, Beijing, and the Schleswig-Holstein Innovation Fund. R.H. thanks the Fonds der Chemischen Industrie for continuous support. Appendix A

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Research Areas and Centers

Academic Focus: Center for Infection and Inflammation Research (ZIEL)

Coronavirus related work

Research on SARS-CoV-2 / COVID-19

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10.1016/j.bbrc.2007.10.081

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abstract = "Caused by a new coronavirus, severe acute respiratory syndrome (SARS) is a highly contagious disease associated with significant fatality that emerged in 2003. The molecular cause of the unusually high human pathogenicity of the SARS coronavirus (SARS-CoV) is still unknown. In an effort to characterize molecular components of the virus that are absent in other coronaviruses, all of which are considerably less pathogenic for humans, we recombinantly produced the SARS-unique domain (SUD) within non-structural protein 3 (Nsp3) of SARS-CoV and characterized its nucleic-acid binding properties. Zone-interference gel electrophoresis and electrophoretic mobility shift assays revealed a specific affinity of SUD for oligo(G)-strings. A few such segments are present in the SARS-CoV genome, but also in mRNAs of host proteins involved in the regulation of signaling pathways. A putative role of SUD in virus-induced apoptosis or survival of host cells is discussed.",

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AU - Tan, Jinzhi

AU - Kusov, Yuri

AU - Mutschall, Doris

AU - Tech, Stefanie

AU - Nagarajan, Krishna

AU - Hilgenfeld, Rolf

AU - Schmidt, Christian L.

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AB - Caused by a new coronavirus, severe acute respiratory syndrome (SARS) is a highly contagious disease associated with significant fatality that emerged in 2003. The molecular cause of the unusually high human pathogenicity of the SARS coronavirus (SARS-CoV) is still unknown. In an effort to characterize molecular components of the virus that are absent in other coronaviruses, all of which are considerably less pathogenic for humans, we recombinantly produced the SARS-unique domain (SUD) within non-structural protein 3 (Nsp3) of SARS-CoV and characterized its nucleic-acid binding properties. Zone-interference gel electrophoresis and electrophoretic mobility shift assays revealed a specific affinity of SUD for oligo(G)-strings. A few such segments are present in the SARS-CoV genome, but also in mRNAs of host proteins involved in the regulation of signaling pathways. A putative role of SUD in virus-induced apoptosis or survival of host cells is discussed.

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The "SARS-unique domain" (SUD) of SARS coronavirus is an oligo(G)-binding protein

Abstract

Funding

UN SDGs

Research Areas and Centers

Coronavirus related work

Access to Document

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