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
16 Citations (Scopus)


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 languageEnglish
JournalBiochemical and Biophysical Research Communications
Issue number4
Pages (from-to)877-882
Number of pages6
Publication statusPublished - 28.12.2007

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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