Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học quốc tế cung cấp cho các bạn kiến thức về ngành y đề tài: Evolution of the HIV-1 envelope glycoproteins with a disulfide bond between gp120 and gp41 | Retrovirology BioMed Central Research Open Access Evolution of the HIV-I envelope glycoproteins with a disulfide bond between gp120 and gp41 Rogier W Sanders1 2 Martijn M Dankers1 Els Busser1 Michael Caffrey3 John P Moore2 and Ben Berkhout 1 Address 1Dept. of Human Retrovirology Academic Medical Center University of Amsterdam 1105 AZ Amsterdam The Netherlands 2Dept. of Microbiology and Immunology Weill Medical College of Cornell University 1300 York Ave. New York NY 1002 USA and 3Dept. of Biochemistry and Molecular Biology University of Illinois at Chicago Chicago IL 60612 USA Email Rogier W Sanders - Martijn M Dankers - mdankers@ Els Busser - eisje@ Michael Caffrey - caffrey@ John P Moore - jpm2003@ Ben Berkhout - Corresponding author Published 09 March 2004 Received 23 February 2004 Accepted 09 March 2004 Retrovirology 2004 1 3 This article is available from http content 1 1 3 2004 Sanders et al licensee BioMed Central Ltd. This is an Open Access article verbatim copying and redistribution of this article are permitted in all media for any purpose provided this notice is preserved along with the article s original URL. Abstract Background We previously described the construction of an HIV-1 envelope glycoprotein complex Env that is stabilized by an engineered intermolecular disulfide bond SOS between gp 1 20 and gp41. The modified Env protein antigenically mimics the functional wild-type Env complex. Here we explore the effects of the covalent gp120 - gp4 1 interaction on virus replication and evolution. Results An HIV-1 molecular clone containing the SOS Env gene was only minimally replication competent suggesting that the engineered disulfide bond substantially impaired Env function. However virus evolution occurred in cell culture infections and it eventually always led to elimination of the intermolecular disulfide bond. In the course of these .