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dc.contributor.authorSrivastava, Sarika Kumari
dc.creatorSrivastava, Sarika Kumarien_US
dc.date.accessioned2012-09-18T20:43:18Z
dc.date.available2012-09-18T20:43:18Z
dc.date.issued2012-05
dc.identifier.citationSrivastava, Sarika Kumari. (2012). A Glimpse into the Role and Mechanism of UL135 in HCMV Apoptosis (Bachelor's thesis, University of Arizona, Tucson, USA).
dc.identifier.urihttp://hdl.handle.net/10150/244786
dc.description.abstractHuman cytomegalovirus (HCMV) exists indefinitely in infected individuals through a latent infection that is poorly characterized in hematopoetic cells. We have previously demonstrated that the UL133-UL138 locus within the ULb' region encodes proteins that are integral membrane proteins that are co-localized to the Golgi and are involved in the regulation of viral replication. UL135 is of interest in that it is predicted to activate viral replication. Given preliminary results, exogenous expression of UL135 outside of the context of infection results in apoptosis in fibroblasts through caspase pathways. UL135 possesses five SH3 domain binding sites; we hypothesize that UL135 functions through its interaction with SH3 domain-containing proteins. To confirm the importance of the SH3 domain binding sites, I mutated three of the five SH3 domain binding sites both individually and collectively. Preliminary studies show that UL135 exhibits decreased ability to induce apoptosis when the SH3 domain binding sites are mutated, which suggests that UL135 is indeed acting to activate viral replication by suppressing UL138, a protein previously identified as necessary in establishing a latent infection. Future directions include repetition of these preliminary experiments in addition to creating viruses with these mutants in order to analyze their effect on latency during infection.
dc.language.isoenen_US
dc.publisherThe University of Arizona.en_US
dc.rightsCopyright © is held by the author. Digital access to this material is made possible by the University Libraries, University of Arizona. Further transmission, reproduction or presentation (such as public display or performance) of protected items is prohibited except with permission of the author.en_US
dc.rights.urihttp://rightsstatements.org/vocab/InC/1.0/
dc.titleA Glimpse into the Role and Mechanism of UL135 in HCMV Apoptosisen_US
dc.typetexten_US
dc.typeElectronic Thesisen_US
thesis.degree.grantorUniversity of Arizonaen_US
thesis.degree.levelbachelorsen_US
thesis.degree.disciplineHonors Collegeen_US
thesis.degree.disciplineMolecular and Cellular Biologyen_US
thesis.degree.nameB.S.en_US
refterms.dateFOA2018-07-06T09:34:35Z
html.description.abstractHuman cytomegalovirus (HCMV) exists indefinitely in infected individuals through a latent infection that is poorly characterized in hematopoetic cells. We have previously demonstrated that the UL133-UL138 locus within the ULb' region encodes proteins that are integral membrane proteins that are co-localized to the Golgi and are involved in the regulation of viral replication. UL135 is of interest in that it is predicted to activate viral replication. Given preliminary results, exogenous expression of UL135 outside of the context of infection results in apoptosis in fibroblasts through caspase pathways. UL135 possesses five SH3 domain binding sites; we hypothesize that UL135 functions through its interaction with SH3 domain-containing proteins. To confirm the importance of the SH3 domain binding sites, I mutated three of the five SH3 domain binding sites both individually and collectively. Preliminary studies show that UL135 exhibits decreased ability to induce apoptosis when the SH3 domain binding sites are mutated, which suggests that UL135 is indeed acting to activate viral replication by suppressing UL138, a protein previously identified as necessary in establishing a latent infection. Future directions include repetition of these preliminary experiments in addition to creating viruses with these mutants in order to analyze their effect on latency during infection.


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