Vaccinia virus assembly and motility

Show simple item record

dc.contributor.advisor Cotter, Thomas G. en
dc.contributor.advisor Sheehan, David
dc.contributor.advisor Griffiths, Gareth
dc.contributor.author Cudmore, Sally
dc.date.accessioned 2014-08-19T11:17:30Z
dc.date.available 2014-08-19T11:17:30Z
dc.date.issued 1996
dc.date.submitted 1996
dc.identifier.citation Cudmore, S. 1996. Vaccinia virus assembly and motility. PhD Thesis, University College Cork. en
dc.identifier.uri http://hdl.handle.net/10468/1627
dc.description.abstract Vaccinia 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.format.mimetype application/pdf en
dc.language English en
dc.language.iso en en
dc.publisher University College Cork en
dc.relation.uri http://library.ucc.ie/record=b1255996~S0
dc.rights © 1996, Sally Cudmore. en
dc.rights.uri http://creativecommons.org/licenses/by-nc-nd/3.0/ en
dc.subject Vaccinia replication en
dc.subject Vaccinia core proteins en
dc.subject.lcsh Vaccinia en
dc.subject.lcsh Viruses--Reproduction en
dc.subject.lcsh Virology--Research en
dc.title Vaccinia virus assembly and motility en
dc.title.alternative Tionól agus gluaiseacht an víorais Vaccinia en
dc.type Doctoral thesis en
dc.type.qualificationlevel Doctoral en
dc.type.qualificationname PhD (Science) en
dc.internal.availability Full text available en
dc.check.info No embargo required en
dc.description.version Accepted Version
dc.description.status Not peer reviewed en
dc.internal.school Biochemistry en
dc.check.type No Embargo Required
dc.check.reason No embargo required en
dc.check.opt-out Not applicable en
dc.thesis.opt-out false
dc.check.embargoformat Not applicable en
ucc.workflow.supervisor cora@ucc.ie


Files in this item

This item appears in the following Collection(s)

Show simple item record

© 1996, Sally Cudmore. Except where otherwise noted, this item's license is described as © 1996, Sally Cudmore.
This website uses cookies. By using this website, you consent to the use of cookies in accordance with the UCC Privacy and Cookies Statement. For more information about cookies and how you can disable them, visit our Privacy and Cookies statement