Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học 'Respiratory Research cung cấp cho các bạn kiến thức về ngành y đề tài: "Common principles and intermediates of viral protein-mediated fusion: the HIV-1 paradigm. | Retrovirology BioMed Central Open Access Review Common principles and intermediates of viral protein-mediated fusion the HIV-1 paradigm Gregory B Melikyan Address Institute of Human Virology Department of Microbiology and Immunology University of Maryland School of Medicine 725 W. Lombard St Baltimore MD 21201 USA Email Gregory B Melikyan - gmelikian@ Published 10 December 2008 Received II November 2008 Accepted 10 December 2008 Retrovirology 2008 5 111 doi 1742-4690-5- 111 This article is available from http content 5 1 111 2008 Melikyan 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 Enveloped viruses encode specialized fusion proteins which promote the merger of viral and cell membranes permitting the cytosolic release of the viral cores. Understanding the molecular details of this process is essential for antiviral strategies. Recent structural studies revealed a stunning diversity of viral fusion proteins in their native state. In spite of this diversity the post-fusion structures of these proteins share a common trimeric hairpin motif in which the amino- and carboxy-terminal hydrophobic domains are positioned at the same end of a rod-shaped molecule. The converging hairpin motif along with biochemical and functional data implies that disparate viral proteins promote membrane merger via a universal cast-and-fold mechanism. According to this model fusion proteins first anchor themselves to the target membrane through their hydrophobic segments and then fold back bringing the viral and cellular membranes together and forcing their merger. However the pathways of protein refolding and the .
