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Báo cáo y học: " Studies on membrane topology, N-glycosylation and functionality of SARS-CoV membrane prote"

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Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Studies on membrane topology, N-glycosylation and functionality of SARS-CoV membrane prote | Virology Journal BioMed Central Research Studies on membrane topology N-glycosylation and functionality of SARS-CoV membrane protein Daniel VoE1 2 Susanne Pfefferle3 Christian Drosten3 4 Lea Stevermann1 Elisabetta Traggiai5 Antonio Lanzavecchia5 and Stephan Becker 1 Address institute of Virology Philipps-University Marburg 35043 Marburg Germany 2Robert Koch-Institute 13353 Berlin Germany 3Clinical Virology Bernhard-Nocht Institute for Tropical Medicine 20359 Hamburg 4University of Bonn Medical Centre Institute of Virology 53127 Bonn German Germany and institute for Research in Biomedicine CH 6500 Bellinzona Switzerland Email Daniel Vofi - vossd@rki.de Susanne Pfefferle - pfefferle@bni-hamburg.de Christian Drosten - drosten@bni-hamburg.de Lea Stevermann - Lea.Stevermann@gmx.de Elisabetta Traggiai - elisabetta.traggiai@gmail.com Antonio Lanzavecchia - lanzavecchia@irb.unisi.ch Stephan Becker - becker@staff.uni-marburg.de Corresponding author Open Access Published 18 June 2009 Received 22 May 2009 Virology Journal 2009 6 79 doi 10.1186 1743-422X-6-79 Accepted 18 June 2009 This article is available from http www.virologyj.eom content 6 1 79 2009 VoB et al licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License http creativecommons.org licenses by 2.0 which permits unrestricted use distribution and reproduction in any medium provided the original work is properly cited. Abstract__ The glycosylated membrane protein M of the severe acute respiratory syndrome associated coronavirus SARS-CoV is the main structural component of the virion and mediates assembly and budding of viral particles. The membrane topology of SARS-CoV M and the functional significance of its N-glycosylation are not completely understood as is its interaction with the surface glycoprotein S. Using biochemical and immunofluorescence analyses we .

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