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You searched for +publisher:"Purdue University" +contributor:("Richard Kuhn"). Showing records 1 – 2 of 2 total matches.

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Purdue University

1. Chang, Jinsam. Role of NS1 in virus replication using Dengue virus and West Nile virus chimeras.

Degree: MS, Biological Science, 2015, Purdue University

The flavivirus non-structural protein 1 (NS1) is translocated into the endoplasmic reticulum (ER), glycosylated, and secreted from the infected cell. Among its various functions, a role of NS1 in RNA synthesis has been reported. The NS1 has three domains; “β-roll”, “wing” and “β-ladder (spaghetti loop)” domain. The characterization of the three domains of NS1 may help us to understand the multiple functions of NS1 in the context of specific regions of the protein. In this study, we have constructed chimeric Dengue/West Nile (DENV/WNV) viruses, which each contain one of the three domains of NS1 from WNV in a DENV genetic background. The chimeras were characterized with respect to viral RNA synthesis, trans-complementation and virion assembly. It was observed that the β-roll chimera was impaired in RNA synthesis, leading to decreased production of viral particles. The reciprocal chimera, WNV/DENV β-roll chimera also showed a reduced level of replication. The spaghetti loop chimera was defective in viral RNA synthesis, and formed small plaques. The wing domain chimera did not show viral RNA synthesis. Remarkably this chimera was rescued by mutations in the wing domain. Collectively, the results indicate that these three domains have a role in viral RNA synthesis. The wing domain is not interchangeable between DENV and WNV for DENV RNA replication, while β-roll and spaghetti loop chimeras could support RNA synthesis. Advisors/Committee Members: Richard Kuhn, Richard Kuhn, Cynthia Stauffacher, Jason Lanman.

Subjects/Keywords: chimera; Dengue Virus; Non structural protein 1; West Nile Virus

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Chang, J. (2015). Role of NS1 in virus replication using Dengue virus and West Nile virus chimeras. (Thesis). Purdue University. Retrieved from https://docs.lib.purdue.edu/open_access_theses/1172

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16th Edition):

Chang, Jinsam. “Role of NS1 in virus replication using Dengue virus and West Nile virus chimeras.” 2015. Thesis, Purdue University. Accessed January 24, 2020. https://docs.lib.purdue.edu/open_access_theses/1172.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7th Edition):

Chang, Jinsam. “Role of NS1 in virus replication using Dengue virus and West Nile virus chimeras.” 2015. Web. 24 Jan 2020.

Vancouver:

Chang J. Role of NS1 in virus replication using Dengue virus and West Nile virus chimeras. [Internet] [Thesis]. Purdue University; 2015. [cited 2020 Jan 24]. Available from: https://docs.lib.purdue.edu/open_access_theses/1172.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Chang J. Role of NS1 in virus replication using Dengue virus and West Nile virus chimeras. [Thesis]. Purdue University; 2015. Available from: https://docs.lib.purdue.edu/open_access_theses/1172

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation


Purdue University

2. Kesari, Aditi. Factors affecting transduction efficiency of pseudotyped viral vectors incorporating alphaviral glycoproteins.

Degree: PhD, Biological Science, 2016, Purdue University

The genome of an organism has the complete set of biochemical instructions required for sustenance of life. Mutations or abnormalities in this genome lead to genetic disorders. Currently available therapeutic options mostly focus on treating the symptoms, but not curing them. Gene therapy promises to be a curative form of medicine. In gene therapy cells carrying a defective gene are targeted and replaced with a healthy copy of that gene. The vehicles used for delivering this gene are known as vectors. Retroviruses are popularly used gene therapy/transfer vectors. However, retroviruses are limited in the range of cells they can enter and infect. The range of cells targeted by the viral vector can be either expanded or narrowed by replacing the envelope of the virus with the envelope of another virus that has the desired range of tissue tropism. Such hybrid viruses are called pseudotyped viruses. Previously, we have pseudotyped Moloney Murine Leukemia Virus (MoMuLV), a retrovirus with the envelope of Ross River Virus (RRV), an alphavirus. Here, we substituted amino-acid residues of RR-envelope glycoprotein with basic amino-acid residues. We show that this makes the pseudotyped virus utilize heparan sulfate, a ubiquitous molecule present on the surfaces of most cells, as an attachment factor. Attachment to cellular heparan sulfate helps in concentration of virus particles on the cell surface and thus enhancing their chances of cell entry, thereby increasing their transduction efficiency of this viral vector. The same affinity towards heparan sulfate, however, poses a challenge in terms of release of this pseudotyped virus from the producer cells. General principles concerning viral adaptation to the use of attachment factors and improving pseudotyped virus titers through modifying cell membrane components can be derived from these results. We also show that alphavirus-glycoprotein retroviral pseudotypes require cholesterol for entry into the cells. Furthermore, excess cholesterol in cells facilitates the entry of alphavirus-glycoprotein retroviral pseudotypes. We show that alphavirus-glycoprotein pseudotypes transduce the acid sphingomyelinase deficient (ASMase-/-) cells derived from Niemann Pick’s disease-model mice more efficiently than the cells from healthy mice (ASMase+/+). Thus alphavirus-glycoprotein pseudotypes hold a potential as suitable vectors for gene therapy/ transfer in Niemann Pick’s Disease-Type A, a genetic lipid-storage disorder. Advisors/Committee Members: David A. Sanders, David A. Sanders, Peter Hollenbeck, Richard Kuhn, James Leary.

Subjects/Keywords: Biological sciences; Alphaviral glycoproteins; Cholesterol; Heparan sulfate; Niemann Pick's disease; Pseudotyped virus; Viral vectors; Genetics and Genomics; Virology

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APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6th Edition):

Kesari, A. (2016). Factors affecting transduction efficiency of pseudotyped viral vectors incorporating alphaviral glycoproteins. (Doctoral Dissertation). Purdue University. Retrieved from https://docs.lib.purdue.edu/open_access_dissertations/666

Chicago Manual of Style (16th Edition):

Kesari, Aditi. “Factors affecting transduction efficiency of pseudotyped viral vectors incorporating alphaviral glycoproteins.” 2016. Doctoral Dissertation, Purdue University. Accessed January 24, 2020. https://docs.lib.purdue.edu/open_access_dissertations/666.

MLA Handbook (7th Edition):

Kesari, Aditi. “Factors affecting transduction efficiency of pseudotyped viral vectors incorporating alphaviral glycoproteins.” 2016. Web. 24 Jan 2020.

Vancouver:

Kesari A. Factors affecting transduction efficiency of pseudotyped viral vectors incorporating alphaviral glycoproteins. [Internet] [Doctoral dissertation]. Purdue University; 2016. [cited 2020 Jan 24]. Available from: https://docs.lib.purdue.edu/open_access_dissertations/666.

Council of Science Editors:

Kesari A. Factors affecting transduction efficiency of pseudotyped viral vectors incorporating alphaviral glycoproteins. [Doctoral Dissertation]. Purdue University; 2016. Available from: https://docs.lib.purdue.edu/open_access_dissertations/666

.