Heparin binding sites on Ross River virus revealed by electron cryo-microscopy |
| |
Authors: | Zhang Wei Heil Marintha Kuhn Richard J Baker Timothy S |
| |
Affiliation: | Department of Biological Sciences, Purdue University, West Lafayette, IN 47907-2054, USA. |
| |
Abstract: | Cell surface glycosaminoglycans play important roles in cell adhesion and viral entry. Laboratory strains of two alphaviruses, Sindbis and Semliki Forest virus, have been shown to utilize heparan sulfate as an attachment receptor, whereas Ross River virus (RRV) does not significantly interact with it. However, a single amino acid substitution at residue 218 in the RRV E2 glycoprotein adapts the virus to heparan sulfate binding and expands the host range of the virus into chicken embryo fibroblasts. Structures of the RRV mutant, E2 N218R, and its complex with heparin were determined through the use of electron cryo-microscopy and image reconstruction methods. Heparin was found to bind at the distal end of the RRV spikes, in a region of the E2 glycoprotein that has been previously implicated in cell-receptor recognition and antibody binding. |
| |
Keywords: | Alphavirus Ross River virus Heparan sulfate Heparin Electron cryo-microscopy GAG Three-dimensional reconstruction |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|