Báo cáo y học: "Mutation in the loop C-terminal to the cyclophilin A binding site of HIV-1 capsid protein disrupts proper virus assembly and infectivity"

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: "Mutation in the loop C-terminal to the cyclophilin A binding site of HIV-1 capsid protein disrupts proper virus assembly and infectivity. | Retrovirology BioMed Central Short report Open Access Mutation in the loop C-terminal to the cyclophilin A binding site of HIV-I capsid protein disrupts proper virus assembly and infectivity Samir Abdurahman1 Stefan Hoglund2 Anders Hoglund2 and Anders Vahlne 1 Address Division of Clinical Microbiology Karolinska Institutet Karolinska University Hospial Stockholm Sweden and 2Department of Biochemistry Biomedical Center Uppsala University Uppsala Sweden Email Samir Abdurahman - Stefan Hoglund - Anders Hoglund - anders_hoglund@ Anders Vahlne - Corresponding author Published 19 March 2007 Received 20 February 2007 Accepted 19 March 2007 Retrovirology 2007 4 19 doi l 742-4690-4-19 This article is available from http content 4 1 19 2007 Abdurahman 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 We have studied the effects associated with two single amino acid substitution mutations in HIV-1 capsid CA the E98A and E187G. Both amino acids are well conserved among all major HIV-1 subtypes. HIV-1 infectivity is critically dependent on proper CA cone formation and mutations in CA are lethal when they inhibit CA assembly by destabilizing the intra and or inter molecular CA contacts which ultimately abrogate viral replication. Glu98 which is located on a surface of a flexible cyclophilin A binding loop is not involved in any intra-molecular contacts with other CA residues. In contrast Glul87 has extensive intra-molecular contacts with eight other CA residues. Additionally Glu187 has been shown to form a salt-bridge with Arg18 of another N-terminal CA monomer in a N-C dimer. However despite proper virus release .

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