Please use this identifier to cite or link to this item: https://scholarbank.nus.edu.sg/handle/10635/160965
Title: Study of HCRSV as nano-materials and structural study of dsRNA recognition by influenza virus A NS 1
Authors: CHENG AO
Keywords: Hibiscus chlorotic ringspot virus; Crystal structure; Virus-based nano-material; Influenza A virus; Nonstructural protein 1(NS1A); dsRNA recognition
Issue Date: 19-Jan-2009
Citation: CHENG AO (2009-01-19). Study of HCRSV as nano-materials and structural study of dsRNA recognition by influenza virus A NS 1. ScholarBank@NUS Repository.
Abstract: 

THE STUDIES IN THIS THESIS WERE MAINLY INVOLVED IN STRUCTURES OF A VIRUS (HCRSV) AND A VIRAL PROTEIN (NS1A). HIBISCUS CHLOROTIC RINGSPOT VIRUS (HCRSV) IS A POSITIVE SENSE, SINGLE-STRANDED RNA VIRUS BELONGING TO CARMOVIRUS GENUS. HCRSV WAS PURIFIED AND CRYSTALLIZED. THE STRUCTURE OF HCRSV, DETERMINED AT 3.2 ANGSTROM, SHOWED THAT HCRSV USE BETA-ANNULUS AND CA2+ MEDIATION TO STABILIZE ITS CAPSIDS. HCRSV WAS ALSO TRIED TO DEVELOP INTO A MODEL AS VIRUS-BASED NANO-MATERIAL. INFLUENZA A VIRUS NS1A SHIELDS THE VIRUSE AGAINST HOST DEFENSE AS AN IMMUNOSUPPRESSOR. THE COMPLEX CRYSTAL STRUCTURE OF NS1A RNA BINDING DOMAIN (RBD) WITH DSRNA REVEALED THAT NS1A RBD FORMS A DIMERIC SIX-HELICAL FOLD AND USED A DIMERIC ANTI-PARALLEL HELICES TO RECOGNIZE THE MAJOR GROOVE OF THE DSRNA AS A SEQUENCE-INDEPENDENT MODE. THE SIGNIFICANT CONFORMATIONAL CHANGE OF RESIDUE R38 BEFORE AND AFTER NS1A RBD BINDING TO DSRNA INDICATED THAT R38 PLAYED A KEY ROLE FOR DSRNA BINDING.

URI: https://scholarbank.nus.edu.sg/handle/10635/160965
Appears in Collections:Ph.D Theses (Open)

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