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Association of the P6 protein of cauliflower mosaic virus with plasmodesmata and plasmodesmal proteins

dc.contributor.advisorSchoelz, James E. (James Edgar), 1958-eng
dc.contributor.authorRodriguez, Andres, 1984-eng
dc.date.issued2014eng
dc.date.submitted2014 Springeng
dc.description"May 2014."eng
dc.descriptionDissertation Supervisor: Dr. James E. Schoelz.eng
dc.descriptionIncludes vita.eng
dc.description.abstractThe P6 protein of Cauliflower mosaic virus (CaMV) is responsible for the formation of inclusion bodies (IBs), which are the site for viral gene expression, replication and virion assembly. Moreover, recent evidence indicates that ectopically expressed P6 IBs move in association with actin microfilaments. Since CaMV virions accumulate preferentially in P6 IBs, we hypothesized that P6 IBs have a role in delivering CaMV virions to the plasmodesmata. We recently discovered that the P6 protein interacted with a C2 calcium-dependent membrane targeting protein (designated AtSRC2-2) in a yeast two-hybrid screen and confirmed this interaction through co-immunoprecipitation and co-localization assays in the CaMV host, Nicotiana benthamiana. An AtSRC2-2 protein fused to RFP was localized to the plasma membrane and specifically associated with plasmodesmata. The AtSRC2-2-RFP fusion also co-localized with two proteins previously shown to associate with plasmodesmata: the host protein PDLP1 and the CaMV movement protein (MP). Since P6 IBs were found to co-localize with AtSCR2-2 and had previously been shown to interact with CaMV MP, we investigated whether a portion of the P6 IBs might also be associated with plasmodesmata. We examined the co-localization of P6-GFP IBs with PDLP1, the CaMV MP, and with aniline blue, a chemical stain for callose, and found that P6-GFP IBs were associated with each of these markers. Furthermore, a P6-RFP protein was co-immunoprecipitated with PDLP1-GFP. Our evidence that a portion of P6-GFP IBs associate with AtSRC2-2, PDLP1, and CaMV MP at plasmodesmata supports a model in which P6 IBs function to transfer CaMV virions directly to plasmodesmata.eng
dc.description.bibrefIncludes bibliographical references.eng
dc.format.extent1 online resource (3 files) : illustrations (some color)eng
dc.identifier.merlinb107808286eng
dc.identifier.oclc906039406eng
dc.identifier.urihttps://hdl.handle.net/10355/44198
dc.identifier.urihttps://doi.org/10.32469/10355/44198eng
dc.languageEnglisheng
dc.publisher[University of Missouri--Columbia]eng
dc.relation.ispartofcommunityUniversity of Missouri--Columbia. Graduate School. Theses and Dissertationseng
dc.rightsOpenAccesseng
dc.rights.licenseThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 3.0 License.
dc.sourceSubmitted by the University of Missouri--Columbia Graduate Schooleng
dc.subjectAuthor supplied: CaMV; Plasmodesmata; Intracellular Movement; plant virus; AtSRC2.2; PDLP1eng
dc.titleAssociation of the P6 protein of cauliflower mosaic virus with plasmodesmata and plasmodesmal proteinseng
dc.titleAssociation of the P6 protein of cauliflower mosaic virus with plasmodesmata and plasmodesmal proteinseng
dc.typeThesiseng
thesis.degree.disciplinePlant, insect and microbial sciences (MU)eng
thesis.degree.grantorUniversity of Missouri--Columbiaeng
thesis.degree.levelDoctoraleng
thesis.degree.namePh. D.eng


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