tailieunhanh - Báo cáo y học: "Mutagenesis of the transmembrane domain of the SARS coronavirus spike glycoprotein: refinement of the requirements for SARS coronavirus cell entry"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Mutagenesis of the transmembrane domain of the SARS coronavirus spike glycoprotein: refinement of the requirements for SARS coronavirus cell entry | Virology Journal BioMed Central Research Mutagenesis of the transmembrane domain of the SARS coronavirus spike glycoprotein refinement of the requirements for SARS coronavirus cell entry Jeroen Corver Rene Broer Puck van Kasteren and Willy Spaan Open Access Address Department of Medical Microbiology Center of Infectious Diseases Leiden University Medical Center 2300 RC Leiden the Netherlands Email Jeroen Corver - Rene Broer - broer66@ Puck van Kasteren - Willy Spaan - Corresponding author Published 24 December 2009 Received 20 November 2009 Accepted 24 December 2009 Virology Journal 2009 6 230 doi 1743-422X-6-230 This article is available from http content 6 1 230 2009 Corver et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http licenses by which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract Background The spike protein S of SARS Coronavirus SARS-CoV mediates entry of the virus into target cells including receptor binding and membrane fusion. Close to or in the viral membrane the S protein contains three distinct motifs a juxtamembrane aromatic part a central highly hydrophobic stretch and a cysteine rich motif. Here we investigate the role of aromatic and hydrophobic parts of S in the entry of SARS CoV and in cell-cell fusion. This was investigated using the previously described SARS pseudotyped particles system SARSpp and by fluorescence-based cell-cell fusion assays. Results Mutagenesis showed that the aromatic domain was crucial for SARSpp entry into cells with a likely role in pore enlargement. Introduction of lysine residues in the hydrophobic stretch of S also resulted in a block of entry .