Vaccinia virus assembly and motility

Simple item page
dc.check.embargoformatNot applicableen
dc.check.infoNo embargo requireden
dc.check.opt-outNot applicableen
dc.check.reasonNo embargo requireden
dc.check.typeNo Embargo Required
dc.contributor.advisorCotter, Thomas G.en
dc.contributor.advisorSheehan, David
dc.contributor.advisorGriffiths, Gareth
dc.contributor.authorCudmore, Sally
dc.date.accessioned2014-08-19T11:17:30Z
dc.date.available2014-08-19T11:17:30Z
dc.date.issued1996
dc.date.submitted1996
dc.description.abstractVaccinia virus, the prototype member of the orthopoxviruses, is the largest and the most complex virus known. After replication of its genome and expression of the viral proteins, vaccinia undergoes a complicated assembly process which produces two distinct infectious forms. The first of these, the intracellular mature virus (IMV), develops from the immature virion (IV) after packaging of the genome and cleavage of the core proteins. During the transition of the IV to the IMV, a new core structure develops in the centre of the virion, concomitantly with the appearance of spike-like structures which extend between this core and the surrounding membranes of the IMV. I describe the characterization of p39 (gene A4L) which is hypothesized to be one component of these spikes. p39 is a core protein, but has strong associations with the membranes surrounding the IMV, possibly due to an interaction with p21 (A17L). Due to its location between the core and the membranes of the IMV, p39 is ideally situated to act as a matrix-like linker protein and may play a role in the formation of the core during the transition of the IV to the IMV. The IMV is subsequently wrapped by a membrane cisterna derived from the trans Golgi network, to form the intracellular enveloped virus (IEV). I show that the IEV can co-opt the actin cytoskeleton of the host cell in order to induce the formation of actin tails which extend from one side of the virion. These actin tails propel the virus particle, both intra- and intercellularly, at speeds of up to 2.8µm/min. On reaching the plasma membrane, the virus particles project out from the cell surface at the tip of virally induced microvilli. The outer membrane of the IEV is thought to fuse with the plasma membrane at the tip of these projections, thus exposing the second infectious form of vaccinia. This is thought to be the means by which the cell-associated enveloped virus is presented to neighbouring cells, thereby facilitating the direct cell-to-cell spread of virus particles.en
dc.description.statusNot peer revieweden
dc.description.versionAccepted Version
dc.format.mimetypeapplication/pdfen
dc.identifier.citationCudmore, S. 1996. Vaccinia virus assembly and motility. PhD Thesis, University College Cork.en
dc.identifier.urihttps://hdl.handle.net/10468/1627
dc.languageEnglishen
dc.language.isoenen
dc.publisherUniversity College Corken
dc.relation.urihttp://library.ucc.ie/record=b1255996~S0
dc.rights© 1996, Sally Cudmore.en
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/3.0/en
dc.subjectVaccinia replicationen
dc.subjectVaccinia core proteinsen
dc.subject.lcshVacciniaen
dc.subject.lcshViruses--Reproductionen
dc.subject.lcshVirology--Researchen
dc.thesis.opt-outfalse
dc.titleVaccinia virus assembly and motilityen
dc.title.alternativeTionól agus gluaiseacht an víorais Vacciniaen
dc.typeDoctoral thesisen
dc.type.qualificationlevelDoctoralen
dc.type.qualificationnamePhD (Science)en
ucc.workflow.supervisorcora@ucc.ie
Files
Original bundle
Now showing 1 - 2 of 2
Thumbnail Image
Name:
CudmoreS_PhDThesis1996.pdf
Size:
39.94 MB
Format:
Adobe Portable Document Format
Description:
Full Text E-thesis
Download
Thumbnail Image
Name:
CudmoreS_PhDThesis1996_.zip
Size:
252.16 MB
Format:
http://www.iana.org/assignments/media-types/application/zip
Description:
Original Scanned Files
License bundle
Now showing 1 - 1 of 1
Thumbnail Image
Name:
license.txt
Size:
5.62 KB
Format:
Item-specific license agreed upon to submission
Description:
Download
Collections
Doctoral Theses
Biochemistry and Cell Biology - Doctoral Theses
College of Science, Engineering and Food Science - Doctoral Theses