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Báo cáo hóa học: " The herpes simplex virus UL20 protein functions in glycoprotein K (gK) intracellular transport and virus-induced cell fusion are independent of UL20 functions in cytoplasmic virion envelopment"

Tham khảo tài liệu 'báo cáo hóa học: " the herpes simplex virus ul20 protein functions in glycoprotein k (gk) intracellular transport and virus-induced cell fusion are independent of ul20 functions in cytoplasmic virion envelopment"', luận văn - báo cáo phục vụ nhu cầu học tập, nghiên cứu và làm việc hiệu quả | Virology Journal BioMed Central Open Access The herpes simplex virus UL20 protein functions in glycoprotein K gK intracellular transport and virus-induced cell fusion are independent of UL20 functions in cytoplasmic virion envelopment Jeffrey M Melancon Preston A Fulmer and Konstantin G Kousoulas Address Division of Biotechnology and Molecular Medicine School of Veterinary Medicine Louisiana State University Baton Rouge USA Email Jeffrey M Melancon - jmelan@lsuhsc.edu Preston A Fulmer - preston.fulmer@nrl.navy.mil Konstantin G Kousoulas - vtgusk@lsu.edu Corresponding author Published 8 November 2007 Received 19 October 2007 Accepted 8 November 2007 Virology Journal 2007 4 120 doi l0.ll86 l743-422X-4-l20 This article is available from http www.virologyj.com content 4 l l20 2007 Melancon 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 HSV-l UL20 protein UL20p and glycoprotein K gK are both important determinants of cytoplasmic virion morphogenesis and virus-induced cell fusion. In this manuscript we examined the effect of UL20 mutations on the coordinate transport and Trans Golgi Network TGN localization of UL20p and gK virus-induced cell fusion and infectious virus production. Deletion of l8 amino acids from the UL20p carboxyl terminus UL20 mutant 204t inhibited intracellular transport and cell-surface expression of both gK and UL20 resulting in accumulation of UL20p and gK in the endoplasmic reticulum ER in agreement with the inability of 204t to complement UL20-null virus replication and virus-induced cell fusion. In contrast less severe carboxyl terminal deletions of either ll or six amino acids UL20 mutants 2llt and 2l6t respectively allowed efficient UL20p and gK intracellular transport cell-surface .