tailieunhanh - Báo cáo y học: " A single site for N-linked glycosylation in the envelope glycoprotein of feline immunodeficiency virus modulates the virus-receptor interaction"

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: " A single site for N-linked glycosylation in the envelope glycoprotein of feline immunodeficiency virus modulates the virus-receptor interaction. | Retrovirology BioMed Central Research A single site for N-linked glycosylation in the envelope glycoprotein of feline immunodeficiency virus modulates the virus-receptor interaction Brian J Willett Elizabeth L McMonagle Nicola Logan Ayman Samman and Margaret J Hosie Open Access Address Retrovirus Research Laboratory Institute of Comparative Medicine Faculty of Veterinary Medicine University of Glasgow Bearsden Road Glasgow G61 1QH UK Email Brian J Willett - Elizabeth L McMonagle - Nicola Logan - Ayman Samman - aymansamman@ Margaret J Hosie - Corresponding author Published 22 August 2008 Received 23 June 2008 Accepted 22 August 2008 Retrovirology 2008 5 77 doi I 742-4690-5-77 This article is available from http content 5 1 77 2008 Willett 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 Feline immunodeficiency virus FIV targets helper T cells by attachment of the envelope glycoprotein Env to CD134 a subsequent interaction with CXCR4 then facilitating the process of viral entry. As the CXCR4 binding site is not exposed until CDl34-binding has occurred then the virus is protected from neutralising antibodies targeting the CXCR4-binding site on Env. Prototypic FIV vaccines based on the FL4 strain of FIV contain a cell culture-adapted strain of FIV Petaluma a CD134-independent strain of FIV that interacts directly with CXCR4. In addition to a characteristic increase in charge in the V3 loop homologue of FIVFL4 we identified two mutations in potential sites for N-linked glycosylation in the region of FIV Env analogous to the VI-V2 region of HIV and SIV Env T27II and N342Y. When these .