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Báo cáo hóa học: " The role of single N-glycans in proteolytic processing and cell surface transport of the Lassa virus glycoprotein GP-C"

Tuyển tập báo cáo các nghiên cứu khoa học quốc tế ngành hóa học dành cho các bạn yêu hóa học tham khảo đề tài: The role of single N-glycans in proteolytic processing and cell surface transport of the Lassa virus glycoprotein GP-C | Virology Journal BioMed Central Research Open Access The role of single N-glycans in proteolytic processing and cell surface transport of the Lassa virus glycoprotein GP-C Robert Eichler1 2 Oliver Lenz1 3 Wolfgang Garten 1 and Thomas Strecker1 Address 1Institut fur Virologie der Philipps-Universitat Marburg Hans-Meerwein-Str. 3 35037 Marburg Germany 2Abbott GmbH Co KG Max-Planck-Ring 2 65205 Wiesbaden Germany and 3Tibotec BVBA Gen De Wittelaan L 11B 3 2800 Mechelen Belgium Email Robert Eichler - Robert.Eichler@abbott.com Oliver Lenz - olenz@tibbe.jnj.com Wolfgang Garten - garten@staff.uni-marburg.de Thomas Strecker - strecker@staff.uni-marburg.de Corresponding author Published 31 May 2006 Received 01 February 2006 Accepted 3 I May 2006 Virology Journal 2006 3 41 doi 10.1186 1743-422X-3-41 This article is available from http www.virologyj.com content 3 I 4I 2006 Eichler 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 Lassa virus glycoprotein is synthesised as a precursor preGP-C into the lumen of the endoplasmic reticulum. After cotranslational cleavage of the signal peptide the immature GP-C is posttranslationally processed into the N-terminal subunit GP-1 and the C-terminal subunit GP-2 by the host cell subtilase SKI-1 S1P. The glycoprotein precursor contains eleven potential N-glycosylation sites. In this report we investigated the effect of each N-glycan on proteolytic cleavage and cell surface transport by disrupting the consensus sequences of eleven potential N-glycan attachment sites individually. Five glycoprotein mutants with disrupted N-glycosylation sites were still proteolytically processed whereas the remaining N-glycosylation sites are necessary for GP-C cleavage. Despite the lack of proteolytic