Structural and Functional Studies on the Infectious Salmon Anemia Virus Nucleoprotein

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dc.contributor.advisorTao, Yizhi Janeen_US
dc.contributor.committeeMemberBeckingham, Kathleen M.en_US
dc.contributor.committeeMemberNikonowicz, Edward P.en_US
dc.contributor.committeeMemberSuh, Junghaeen_US
dc.contributor.committeeMemberWang, Qinghuaen_US
dc.creatorZheng, Wenjieen_US
dc.date.accessioned2014-10-17T16:32:52Zen_US
dc.date.available2014-10-17T16:32:52Zen_US
dc.date.created2013-12en_US
dc.date.issued2013-10-25en_US
dc.date.submittedDecember 2013en_US
dc.date.updated2014-10-17T16:32:53Zen_US
dc.description.abstractGenome packaging for viruses with segmented genomes is often a complex problem. This is particularly true for influenza viruses and other orthomyxoviruses which are able to cause infectious disease, and even worldwide pandemics. The genome of Orthomyxovirus consists of 6-8 negative-sense RNAs encapsidated as ribonucleoprotein (RNP) complexes which perform multiple essential functions throughout the virus life cycle. To better understand the structural features of orthomyxovirus RNPs that allow them to be specifically packaged, we performed structural/functional studies of the nucleoprotein (NP), the major protein component of the RNPs, from the infectious salmon anemia virus (ISAV). The crystal structure of the ISAV-NP was determined to 2.7Å resolution. The ISAV-NP possesses a 112-aa N-terminal domain and a bi-lobular core structure that strongly resembles the structure of the influenza virus NP. Because the ISAV-NP forms homogenous dimers that are stable in solution, I was able to study the NP:RNA binding affinity as well as stoichiometry with fluorescence polarization, using recombinant proteins and synthetic oligos. Surprisingly, the RNA binding analysis revealed that each NP binds ~12 nts of RNA, shorter than the 24-28 nts originally estimated for the influenza A virus NP. The 12-nt stoichiometry was further confirmed by results from electron microscopy and dynamic light scattering. These results suggest that free RNA exists in the orthomyxovirus RNPs, and selective RNP packaging is likely accomplished through direct RNA-RNA interactions.en_US
dc.format.mimetypeapplication/pdfen_US
dc.identifier.citationZheng, Wenjie. "Structural and Functional Studies on the Infectious Salmon Anemia Virus Nucleoprotein." (2013) Diss., Rice University. <a href="https://hdl.handle.net/1911/77601">https://hdl.handle.net/1911/77601</a>.en_US
dc.identifier.urihttps://hdl.handle.net/1911/77601en_US
dc.language.isoengen_US
dc.rightsCopyright is held by the author, unless otherwise indicated. Permission to reuse, publish, or reproduce the work beyond the bounds of fair use or other exemptions to copyright law must be obtained from the copyright holder.en_US
dc.subjectInfluenzaen_US
dc.subjectNucleoproteinen_US
dc.subjectRibonucleoproteinen_US
dc.subjectGenomic packagingen_US
dc.subjectX-ray crystallographyen_US
dc.subjectIsavirusen_US
dc.subjectBiophysicsen_US
dc.titleStructural and Functional Studies on the Infectious Salmon Anemia Virus Nucleoproteinen_US
dc.typeThesisen_US
dc.type.materialTexten_US
thesis.degree.departmentBiochemistry and Cell Biologyen_US
thesis.degree.disciplineNatural Sciencesen_US
thesis.degree.grantorRice Universityen_US
thesis.degree.levelDoctoralen_US
thesis.degree.nameDoctor of Philosophyen_US
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