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You searched for +publisher:"Purdue University" +contributor:("Jason Lanman"). Showing records 1 – 3 of 3 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 (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. Yu, Guimei. Affinity cryo-electron microscopy: Methods development and applications.

Degree: PhD, Biological Science, 2016, Purdue University

Single particle cryo-electron microscopy (cryo-EM) is an emerging powerful tool for structural studies of macromolecular assemblies. Although less concentrated and smaller amounts of samples are required for single particle cryo-EM compared to X-ray crystallography, it remains challenging to study specimens that are low-abundance, low-yield, or short-lived. The recent development of affinity grid techniques holds great promise to tackle these challenging samples by combining the sample purification and freezing on TEM grids steps in cryo-EM grid preparation into a single step, revolutionize the grid preparation of cryo-EM, and extend single particle cryo-EM to a routine structural biology tool to characterize structures of a broad spectrum of macromolecules. In my PhD study, I have established a new design of the affinity cryo-EM approach, cryo-SPIEM that applies a traditional pathogen diagnosis tool Solid Phase Immune Electron Microscopy (SPIEM) to the single particle cryo-EM method, and also systematically explored the applications of affinity EM approaches and the potentials of affinity cryo-EM approaches for near-atomic single particle 3-D reconstruction. The cryo-SPIEM approach provides an alternative, largely simplified and easier to use affinity grid that directly works with most native macromolecular complexes with established antibodies, and enables cryo-EM studies of native samples directly from cell cultures. The application of the affinity cryo-EM approach for high-resolution cryo-EM has been demonstrated successfully by solving a 6.3 Å structure of Tulane virus using the polylysine-based affinity grid, and a 2.6 Å structure of Tulane virus using the antibody-based affinity grid with a sample of low concentrations that defies standard cryo-EM study. Moreover, we have applied the affinity grid technique to investigate the interaction between Tulane virus and its cellular receptor Histo-blood group antigens, which revealed the potential roles of HBGA receptors in mediating genome release. Advisors/Committee Members: Wen Jiang, Wen Jiang, Richard J. Kuhn, Jason Lanman, Chiwook Park.

Subjects/Keywords: Biophysics; Microbiology; Molecular Biology

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APA (6th Edition):

Yu, G. (2016). Affinity cryo-electron microscopy: Methods development and applications. (Doctoral Dissertation). Purdue University. Retrieved from https://docs.lib.purdue.edu/open_access_dissertations/1041

Chicago Manual of Style (16th Edition):

Yu, Guimei. “Affinity cryo-electron microscopy: Methods development and applications.” 2016. Doctoral Dissertation, Purdue University. Accessed January 24, 2020. https://docs.lib.purdue.edu/open_access_dissertations/1041.

MLA Handbook (7th Edition):

Yu, Guimei. “Affinity cryo-electron microscopy: Methods development and applications.” 2016. Web. 24 Jan 2020.

Vancouver:

Yu G. Affinity cryo-electron microscopy: Methods development and applications. [Internet] [Doctoral dissertation]. Purdue University; 2016. [cited 2020 Jan 24]. Available from: https://docs.lib.purdue.edu/open_access_dissertations/1041.

Council of Science Editors:

Yu G. Affinity cryo-electron microscopy: Methods development and applications. [Doctoral Dissertation]. Purdue University; 2016. Available from: https://docs.lib.purdue.edu/open_access_dissertations/1041

3. Sequra, Jason Michael. Investigating the effects of pH on alphaviral E3-E2 glycoprotein association, organization, and cellular tropism.

Degree: PhD, Biological Science, 2016, Purdue University

In alphaviruses the role of E3 is required in protecting the fusion peptide region of E1 during intracellular transport. Throughout viral processing, the association of E2 and E3 is required for the successful trafficking and incorporation of E1 into the mature virion. This E3-E2 association has been observed to extend to mature virions in the solved structure for the envelope of Semliki Forest virus (SFV) and supported by the solved structure for the entire Venezuelan equine encephalitis virion (VEEV) with exclusive contacts being made between E3-E2. Immunization with monoclonal antibodies against VEEV E3 provided protection for mice challenged by lethal doses of VEEV and suggests potential new targets for antibody neutralization, but it is currently unclear if E3 is retained on mature VEEV virus. Using non-replicating expression systems that avoid virus-culturing artifacts, we discovered that Moloney murine leukemia virus or baculovirus pseudotyped with the alphavirus envelope spike complex of VEEV demonstrates a pH-dependent retention of E3 on mature virus for both mammalian cells and insect cells through indirect-immunofluorescence assays and neutralization studies using polyclonal antibodies against VEEV E3. In studies investigating the impacts of retaining the E3 glycoprotein on mature virus outside of a host cell, we found this retention of E3 decreases receptor-mediated entry of cell targets that can be rescued on cells containing heparan sulfate suggesting viruses containing E3 on mature envelopes can utilize the E3 protein as an attachment factor. We utilized a method for downregulating the cell-surface expression of the natural resistance-associated macrophage protein (NRAMP2), a definitive receptor for the prototypic alphavirus Sindbis (SIND), on cellular targets. We observed a significant decrease in entry of VEEV versus control Ross River (RRV) virus that does not utilize NRAMP2. This inhibition can be rescued with binding to heparan sulfate by VEEV retaining E3. Together, these data suggest that the E3 glycoprotein protects the fusion region of E1 on budded, mature virus dependent on the pH of the extracellular environment. This association potentially serves a role as an attachment factor on virus and presents new binding sites for protein interactions and potential inhibition. Advisors/Committee Members: Jason Lanman, Jason Lanman, Elizabeth J. Taparowsky, Harm Hogenesch, David A. Sanders.

Subjects/Keywords: Biological sciences; Alphavirus; Heparan sulfate; Membrane fusion; Venezuelan equine encephalitis virus; Viral entry; Viral glycoprotein; Cell Biology; Molecular Biology; Virology

…Segura, Jason M. PhD., Purdue University, December 2016. Investigating the Effects of pH On… …graciously donated by Andy Mesecar (Purdue University, West Lafayette, IN.). CHO 22/18.4… …were graciously donated by Richard Kuhn (Purdue University, West Lafayette, IN.)… 

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

APA (6th Edition):

Sequra, J. M. (2016). Investigating the effects of pH on alphaviral E3-E2 glycoprotein association, organization, and cellular tropism. (Doctoral Dissertation). Purdue University. Retrieved from https://docs.lib.purdue.edu/open_access_dissertations/997

Chicago Manual of Style (16th Edition):

Sequra, Jason Michael. “Investigating the effects of pH on alphaviral E3-E2 glycoprotein association, organization, and cellular tropism.” 2016. Doctoral Dissertation, Purdue University. Accessed January 24, 2020. https://docs.lib.purdue.edu/open_access_dissertations/997.

MLA Handbook (7th Edition):

Sequra, Jason Michael. “Investigating the effects of pH on alphaviral E3-E2 glycoprotein association, organization, and cellular tropism.” 2016. Web. 24 Jan 2020.

Vancouver:

Sequra JM. Investigating the effects of pH on alphaviral E3-E2 glycoprotein association, organization, and cellular tropism. [Internet] [Doctoral dissertation]. Purdue University; 2016. [cited 2020 Jan 24]. Available from: https://docs.lib.purdue.edu/open_access_dissertations/997.

Council of Science Editors:

Sequra JM. Investigating the effects of pH on alphaviral E3-E2 glycoprotein association, organization, and cellular tropism. [Doctoral Dissertation]. Purdue University; 2016. Available from: https://docs.lib.purdue.edu/open_access_dissertations/997

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