خط مشی دسترسیدرباره ماپشتیبانی آنلاین
ثبت نامثبت نام
راهنماراهنما
فارسی
ورودورود
صفحه اصلیصفحه اصلی
جستجوی مدارک
تمام متن
منابع دیجیتالی
رکورد قبلیرکورد بعدی
Document Type:Latin Dissertation
Language of Document:English
Record Number:55717
Doc. No:TL25671
Call number:‭3357509‬
Main Entry:Kai Xu
Title & Author:Host cell recognition by henipavirus crystal structures of henipavirus attachment glycoproteins and the complexes with receptorsKai Xu
College:Weill Medical College of Cornell University
Date:2009
Degree:Ph.D.
student score:2009
Page No:104
Abstract:The henipaviruses, represented by Nipah virus (NiV) and Hendra virus (HeV), are emerging zoonotic paramyxoviruses responsible for repeated outbreaks in humans and animals associated with high morbidity and mortality in Australia, Southeast Asia, India and Bangladesh. Several species of bats, primarily fruit bats of the genus Pteropus have been shown to be the natural host of NiV and HeV. Most human cases of infection have arisen from contact with infected pigs (NiV) or horses (HeV). However, in the more recent outbreaks of NiV in India and Bangladesh, both food-borne and human-to-human transmission was evident. These facts, together with high mortality and morbidity, make the henipaviruses a potential biological agent threat, and there are no available anti-viral therapies for treating NiV or HeV infection. Viral entry has become a very important target for the development of a new generation of anti-viral drugs. The entry of henipavirus is initiated by the attachment of the G envelope glycoprotein (Henipa-G) to host cell membrane receptors (ephrin-B2 or B3), followed by the activation of fusion protein (F), which triggers the fusion between viral envelop and host membrane. The whole process is poorly understood. The molecular details of the interaction between Henipa-G and the ephrins are the key to understanding the first step of the viral infection process. To this end, we have determined the structures of the HeV and NiV G glycoproteins both alone and in complex with their ephrin receptors. Our results reveal the mechanism of G protein mediated host cell recognition in henipavirus and shed lights on the process of the F protein activation. The structures also suggest that designing specific and effective inhibition of the viral attachment step is a feasible approach towards developing specific antiviral drugs.
Subject:Biological sciences; Henipavirus; Ephrin; Crystal; Structure; Virus; Host cell recognition; Glycoproteins; Neurosciences; Virology; 0720:Virology; 0317:Neurosciences
Added Entry:D. Nikolov
Added Entry:Weill Medical College of Cornell University