tailieunhanh - báo cáo hóa học:" The SARS Coronavirus S Glycoprotein Receptor Binding Domain: Fine Mapping and Functional Characterization"

Tuyển tập các báo cáo nghiên cứu về hóa học được đăng trên tạp chí sinh học đề tài : The SARS Coronavirus S Glycoprotein Receptor Binding Domain: Fine Mapping and Functional Characterization | Virology Journal BioMed Central Research Open Access The SARS Coronavirus S Glycoprotein Receptor Binding Domain Fine Mapping and Functional Characterization Samitabh Chakraborti Ponraj Prabakaran Xiaodong Xiao and Dimiter S Dimitrov Address Protein Interactions Group LECB CCR NCI-Frederick NIH Frederick MD 21702-1201 Email Samitabh Chakraborti - schakraborti@ Ponraj Prabakaran - praba@ Xiaodong Xiao - xiaox@ Dimiter S Dimitrov - dimitrov@ Corresponding author Published 25 August 2005 Received 18 July 2005 Accepted 25 August 2005 Virology Journal 2005 2 73 doi 1743-422X-2-73 This article is available from http content 2 1 73 2005 Chakraborti 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 The entry of the SARS coronavirus SCV into cells is initiated by binding of its spike envelope glycoprotein S to a receptor ACE2. We and others identified the receptor-binding domain RBD by using S fragments of various lengths but all including the amino acid residue 318 and two other potential glycosylation sites. To further characterize the role of glycosylation and identify residues important for its function as an interacting partner of ACE2 we have cloned expressed and characterized various soluble fragments of S containing RBD and mutated all potential glycosylation sites and 32 other residues. The shortest of these fragments still able to bind the receptor ACE2 did not include residue 318 which is a potential glycosylation site but started at residue 319 and has only two potential glycosylation sites residues 330 and 357 . Mutation of each of these sites to either alanine or glutamine as well as mutation of residue 318 to alanine in longer fragments