Báo cáo khoa học: " Analysis of a conserved RGE/RGD motif in HCV E2 in mediating entry"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành y học dành cho các bạn tham khảo đề tài: Analysis of a conserved RGE/RGD motif in HCV E2 in mediating entry | Virology Journal BioMed Central Research Analysis of a conserved RGE RGD motif in HCV E2 in mediating entry Katharina B Rothwangl and Lijun Rong Address Department of Microbiology and Immunology University of Illinois at Chicago Chicago IL 60612 USA Email Katharina B Rothwangl - Katharin@ Lijun Rong - lijun@ Corresponding author Open Access Published 26 January 2009 Received 29 October 2008 Accepted 26 January 2009 Virology Journal 2009 6 12 doi l 743-422X-6-12 This article is available from http content 6 1 12 2009 Rothwangl and Rong 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 Hepatitis C virus HCV encodes two transmembrane glycoproteins E1 and E2 which form a heterodimer. E1 is believed to mediate fusion while E2 has been shown to bind cellular receptors. It is clear that HCV uses a multi-receptor complex to gain entry into susceptible cells however key elements of this complex remain elusive. In this study the role of a highly conserved RGE RGD motif of HCV E2 glycoprotein in viral entry was examined. The effect of each substitution mutation in this motif was tested by challenging susceptible cell lines with mutant HCV E1E2 pseudotyped viruses generated using a lentiviral system HCVpp . In addition to assaying infectivity producer cell expression and HCVpp incorporation of HCV E2 proteins CD81 binding profiles and conformation of mutants were examined. Results Based on these characteristics mutants either displayed wt characteristics high infectivity 90 of wt HCVpp CD81 binding E1E2 expression and incorporation into viral particles and proper conformation or very low infectivity 20 of wt HCVpp . Only amino acid substitutions of the 3rd position D or E .

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