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Permanent link (DOI): https://doi.org/10.7939/R3PQ22

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The vaccinia virus N2 protein associates with karyopherins α2 and α4 and reduces the turnover rate of karyopherin α2 Open Access

Descriptions

Other title
Subject/Keyword
Vaccinia Virus
Nuclear Transport
Type of item
Thesis
Degree grantor
University of Alberta
Author or creator
Desaulniers, Megan Amanda
Supervisor and department
Evans, David (Medical Microbiology and Immunology)
Examining committee member and department
Shmulevitz, Maya (Medical Microbiology and Immunology)
Smiley, Jim (Medical Microbiology and Immunology)
Schang, Luis (Biochemistry)
Department
Department of Medical Microbiology and Immunology
Specialization
Virology
Date accepted
2014-09-17T10:57:57Z
Graduation date
2014-11
Degree
Master of Science
Degree level
Master's
Abstract
Due to their large genomes, poxviruses encode a number of enzymes, including a DNA polymerase and a DNA-dependent RNA polymerase, and therefore require few host gene factors for their replication. Several studies have shown several host nuclear factors are in fact recruited to viral sites of replication. Using bioinformatics we identified a putative bipartite nuclear localization signal in vaccinia virus N2L. Through immuno-precipitation, we were able to show that N2 interacts with two nuclear import proteins, karyopherins (KPN) alpha 2 and alpha 4. Immunofluorescence analysis indicated that in the presence of N2, KPNα2 was found evenly dispersed throughout the cell. However, when N2 is absent from the infection, KPNα2 accumulates at the nuclear periphery. Using Fluorescence Recovery After Photobleaching (FRAP), we show that the presence of N2 retards the nuclear turnover rate of KPNα2. Taken together, we suggest that N2 is competing for available KPNα2 to modulate nuclear transport thus promoting virulence.
Language
English
DOI
doi:10.7939/R3PQ22
Rights
Permission is hereby granted to the University of Alberta Libraries to reproduce single copies of this thesis and to lend or sell such copies for private, scholarly or scientific research purposes only. Where the thesis is converted to, or otherwise made available in digital form, the University of Alberta will advise potential users of the thesis of these terms. The author reserves all other publication and other rights in association with the copyright in the thesis and, except as herein before provided, neither the thesis nor any substantial portion thereof may be printed or otherwise reproduced in any material form whatsoever without the author's prior written permission.
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