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Báo cáo y học: "Refined study of the interaction between HIV-1 p6 late domain and ALIX"

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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: "Refined study of the interaction between HIV-1 p6 late domain and ALIX. | Retrovirology BioMed Central Open Access Short report Refined study of the interaction between HIV-1 p6 late domain and ALIX Carine Lazert11 Nathalie Chazal12 Laurence Briant2 Denis Gerlier1 and Jean-Claude Cortay 1 Address 1Université Lyon 1 Centre National de la Recherche Scientifique CNRS VirPatH FRE 3011 Faculte de Médecine RTH Laennec Lyon France and 2Université Montpellier 1 Université Montpellier 2 CNRS Centre d études d agents Pathogènes et Biotechnologies pour la Santé CPBS UMR 5236 F-34965 Montpellier France Email Carine Lazert-carine.lazert@recherche.univ-lyon1.fr Nathalie Chazal - nathalie.chazal@univ-montp1.fr Laurence Briant - laurence.briant@univ-montp1.fr Denis Gerlier - denis.gerlier@univ-lyon1.fr Jean-Claude Cortay - cortay@sante.univ-lyon1.fr Corresponding author fEqual contributors Published 13 May 2008 Received 6 December 2007 Retrovirology 2008 5 39 doi 10.1186 1742-4690-5-39 Accepted 13 May 2008 This article is available from http www.retrovirology.cOm content 5 1 39 2008 Lazert 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 interaction between the HIV-1 p6 late budding domain and ALIX a class E vacuolar protein sorting factor was explored by using the yeast two-hybrid approach. We refined the ALIX binding site of p6 as being the leucine triplet repeat sequence Lxx 4 LYPLTSLRSLFG . Intriguingly the deletion of the C-terminal proline-rich region of ALIX prevented detectable binding to p6. In contrast a four-amino acid deletion in the central hinge region of p6 increased its association with ALIX as shown by its ability to bind to ALIX lacking the proline rich domain. Finally by using a random screening approach the minimal ALIX391_510 fragment was found to specifically interact with

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