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Identification of proteins of the infectious apparatus of Encephalitozoon cuniculi

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TypeOfResource
Text
TitleInfo (ID = T-1)
Title
Identification of proteins of the infectious apparatus of Encephalitozoon cuniculi
SubTitle
PartName
PartNumber
NonSort
Identifier (displayLabel = ); (invalid = )
ETD_2056
Identifier (type = hdl)
http://hdl.rutgers.edu/1782.2/rucore10002600001.ETD.000052274
Language (objectPart = )
LanguageTerm (authority = ISO639-2); (type = code)
eng
Genre (authority = marcgt)
theses
Subject (ID = SBJ-1); (authority = RUETD)
Topic
Biology
Subject (ID = SBJ-2); (authority = ETD-LCSH)
Topic
Nosema cuniculi--Genetics
Subject (ID = SBJ-3); (authority = ETD-LCSH)
Topic
Microsporidia
Abstract
The microsporidia are a diverse phylum of obligate intracellular parasitic protists that infect all major animal groups and have been recognized as emerging human pathogens for which few chemotherapeutic options currently exist. These organisms infect every tissue and organ system, causing significant pathology especially in immune-compromised populations. The microsporidian spore employs a unique infection strategy in which its contents are virtually injected into a host cell via the polar tube, an organelle that lies coiled within the resting spore but erupts with a force sufficient to pierce the plasma membrane of its host cell. It appears that this process is driven by a dramatic osmotic swelling within the spore just prior to germination, which is resisted by the spore wall until the moment of polar filament eruption. Neither the means by which this rapid influx of water across the hydrophobic cell membrane might be supported, nor the molecular structural basis for the elasticity of the polar tube or the tensile strength of the spore wall is well understood. However, the recent sequencing of the genome of human-pathogenic species Encephalitozoon cuniculi has enabled the adoption of genomic and proteomic approaches to address these problems. In the first part of this project, an aquaporin-like gene from this organism (EcAQP) was cloned and the protein subjected to standard functional tests in a heterologous Xenopus oocyte swelling assay. Increased water-permeability and localization of EcAQP to the plasma membrane of transfected oocytes demonstrated the functionality of this gene, suggesting a mechanism for water flux in germinating spores. The second part of this project employed a shotgun-proteomic strategy to identify novel structural components of the microsporidian infectious apparatus. Mass spectrometry of insoluble fractions of spore lysate identified over fifty candidate proteins, many of which were immunolocalized in situ. As a result, novel components of the mitosome, the developing spore wall, and a heretofore unrecognized filamentous network within the lumen of the parasitophorous vacuole were putatively identified. Thus the work described herein generates insights regarding the biochemical events and molecular structural components involved in the infectious process of these unique intracellular pathogens.
PhysicalDescription
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electronic resource
Extent
xvi, 169 p. : ill.
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application/pdf
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text/xml
Note
Supplementary File: Appendices 1, 2, and 3
Note (type = degree)
Ph.D.
Note (type = bibliography)
Includes bibliographical references (p. 150-164)
Note (type = statement of responsibility)
by Kaya Ghosh
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Ghosh
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Kaya
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1976-
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Kaya Ghosh
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Bonder
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Edward
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chair
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Advisory Committee
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Edward Bonder
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Cali
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Ann
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internal member
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Advisory Committee
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Ann Cali
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Kafkewitz
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David
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David Kafkewitz
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Altan-Bonnet
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Nihal
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Advisory Committee
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Nihal Altan-Bonnet
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Weiss
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Louis
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Louis Weiss
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Chan
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John
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outside member
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Advisory Committee
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John Chan
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Rutgers University
Role
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degree grantor
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Graduate School - Newark
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school
OriginInfo
DateCreated (point = ); (qualifier = exact)
2009
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2009-10
Place
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xx
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Title
Rutgers University Electronic Theses and Dissertations
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ETD
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Title
Graduate School - Newark Electronic Theses and Dissertations
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rucore10002600001
Location
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NjNbRU
Identifier (type = doi)
doi:10.7282/T36Q1XD4
Genre (authority = ExL-Esploro)
ETD doctoral
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Rights

RightsDeclaration (AUTHORITY = GS); (ID = rulibRdec0006)
The author owns the copyright to this work.
Copyright
Status
Copyright protected
Availability
Status
Open
Reason
Permission or license
RightsHolder (ID = PRH-1); (type = personal)
Name
FamilyName
Ghosh
GivenName
Kaya
Role
Copyright Holder
RightsEvent (AUTHORITY = rulib); (ID = RE-1)
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Permission or license
DateTime
2009-09-23 16:21:59
AssociatedEntity (AUTHORITY = rulib); (ID = AE-1)
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Copyright holder
Name
Kaya Ghosh
Affiliation
Rutgers University. Graduate School - Newark
Detail
I hereby grant to the Rutgers University Libraries and to my school the non-exclusive right to archive, reproduce and distribute my thesis or dissertation, in whole or in part, and/or my abstract, in whole or in part, in and from an electronic format, subject to the release date subsequently stipulated in this submittal form and approved by my school. I represent and stipulate that the thesis or dissertation and its abstract are my original work, that they do not infringe or violate any rights of others, and that I make these grants as the sole owner of the rights to my thesis or dissertation and its abstract. I represent that I have obtained written permissions, when necessary, from the owner(s) of each third party copyrighted matter to be included in my thesis or dissertation and will supply copies of such upon request by my school. I acknowledge that RU ETD and my school will not distribute my thesis or dissertation or its abstract if, in their reasonable judgment, they believe all such rights have not been secured. I acknowledge that I retain ownership rights to the copyright of my work. I also retain the right to use all or part of this thesis or dissertation in future works, such as articles or books.
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License
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Author Agreement License
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Type
Embargo
DateTime
2010-01-30
Detail
365 days
AssociatedObject (AUTHORITY = rulib); (ID = AO-1)
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Technical

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ETD
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application/pdf
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application/x-tar
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