tailieunhanh - Báo cáo khoa học: On the mechanisms of bananin activity against severe acute respiratory syndrome coronavirus

In a previous study, severe acute respiratory syndrome coronavirus (SARS-CoV) was cultured in the presence of bananin, an effective adamantane-related molecule with antiviral activity. In the present study, we show that all bananin-resistant variants exhibit mutations in helicase and membrane protein, although no evidence of bananin interference on their mutual interaction has been found. | IFEBS Journal On the mechanisms of bananin activity against severe acute respiratory syndrome coronavirus Zai Wang1 Jian-Dong Huang1 Kin-Ling Wong2 Pei-Gang Wang3 Hao-Jie Zhang2 Julian A. Tanner1 Ottavia Spiga4 5 Andrea Bernini4 5 Bo-Jian Zheng2 and Neri Niccolai4 5 1 Department of Biochemistry Faculty of Medicine University of Hong Kong China 2 Department of Microbiology Faculty of Medicine University of Hong Kong China 3 The HKU-Pasteur Research Centre HKU-PRC Pokfulam Hong Kong SAR China 4 Department of Molecular Biology University of Siena Italy 5 SienaBiografix Srl Siena Italy Keywords antiviral drugs bananin coronavirus viral helicase Correspondence . Huang or N. Niccolai Department of Biochemistry University of Hong Kong 3 F Laboratory Block Faculty of Medicine Building 21 Sassoon Road Pokfulam Hong Kong SAR China Department of Molecular Biology University of Siena I-53100 Siena Italy Fax 852 2855 1254 39 0577 234903 Tel 852 2819 2810 39 0577 234910 E-mail jdhuang@ niccolai@ Received 28 June 2010 revised 9 November 2010 accepted 12 November 2010 In a previous study severe acute respiratory syndrome coronavirus SARS-CoV was cultured in the presence of bananin an effective adamantane-related molecule with antiviral activity. In the present study we show that all bananin-resistant variants exhibit mutations in helicase and membrane protein although no evidence of bananin interference on their mutual interaction has been found. A structural analysis on protein sequence mutations found in SARS-CoV bananin-resistant variants was performed. The S259 L mutation of SARS-CoV helicase is always found in all the identified bananin-resistant variants suggesting a primary role of this mutation site for bananin activity. From a structural analysis of SARS-CoV predicted helicase structure S259 is found in a hydrophilic surface pocket far from the enzyme active sites and outside the helicase dimer interface. The S L substitution causes a pocket volume

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