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:Amino acid residues that are important for Hyal2 function as a receptor for jaagsiekte sheep retrovirus | Retrovirology BioMed Central Research Open Access Amino acid residues that are important for Hyal2 function as a receptor for jaagsiekte sheep retrovirus Fuh-Mei Duh1 2 Clarissa Dirks3 4 Michael I Lerman2 and A Dusty Miller 3 Address 1Basic Research Program SAIC-Frederick National Cancer Institute at Frederick Frederick Maryland 21702 USA 2Laboratory of Immunobiology Center for Cancer Research National Cancer Institute at Frederick Frederick Maryland 21702 USA 3Fred Hutchinson Cancer Research Center Seattle Washington 98109 USA and 4Current address University of Washington Seattle Washington 98195 USA Email Fuh-Mei Duh - duh@ Clarissa Dirks - cdirks@ Michael I Lerman - lerman@ A Dusty Miller - dmiller@ Corresponding author Published 28 September 2005 Received 01 September 2005 Accepted 28 September 2005 Retrovirology 2005 2 59 doi 1742-4690-2-59 This article is available from http content 2 1 59 2005 Duh 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 Background Infection by jaagsiekte sheep retrovirus JSRV and by enzootic nasal tumor virus ENTV depends on cell-surface expression of the virus entry receptor hyaluronidase 2 Hyal2 . Human Hyal2 binds the envelope Env proteins of these viruses and is functional as a receptor but Hyal2 from mice does not bind Env nor does it mediate entry of either virus. Here we have explored the amino acid determinants that account for the difference in receptor function. Results Analysis of human-mouse Hyal2 chimeric proteins showed that amino acid differences responsible for the difference in Hyal2 receptor activity were localized to the central third of Hyal2. Human Hyal2 mutants containing .
