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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22Sept09-CHENG Ao PhD Thesis-final version for final submission.pdf | 5.08 MB | Adobe PDF | OPEN | None | View/Download |
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