Fatty acylation of Vaccinia virus proteins : dual myristylation and palmitylation of the A-type inclusion protein Public Deposited

http://ir.library.oregonstate.edu/concern/graduate_thesis_or_dissertations/cn69m675z

Descriptions

Attribute NameValues
Creator
Abstract or Summary
  • The attachment of myristic acid to the N-terminal glycine residue of many eukaryotic and viral proteins is often essential for the acquisition of the protein's biological activity. Vaccinia virus (VV), the prototype member of the Poxviridae, expresses several myristylated proteins during the course of infection. Only one of these proteins, L1R, has been identified and characterized. Experiments were performed to identify and analyze four additional VV myristylproteins. These proteins were identified as the A-type inclusion protein (92 kDa), G9R (39 kDa), A16L (36 kDa), and E7R (17 kDa). The latter three proteins were shown to be myristylated on an N-terminal glycine residue. Additional studies demonstrated that both A16L and E7R are soluble proteins, unlike L1R, which is a constituent of the viral envelope. Furthermore, A16L could not be detected in either purified extracellular enveloped virus (EEV) or in intracellular mature virus (IMV). These are the two predominant forms of infectious virions produced during a VV infection. E7R was detected in EEV and, to a lesser extent, in IMV. Unlike the other proteins, the amino terminal sequence of the A-type inclusion protein did not fit the consensus sequence for N-myristylation (M-G-X-X-X-S/T/A/C/N), suggesting that it was internally myristylated. A combination of studies revealed that the protein is both myristylated and palmitylated. Addition of each acyl group could be separated temporally: myristylation occured co-translationally, while palmitylation occurred post-translationally. Genetic analyses of lysine doublets and arginine/lysine doublets within the A-type inclusion protein indicated that these sites are not utilized for myristylation. This is in contrast to the precursors of TNFoc and Ilia which are internally-myristylated on a lysine doublet. It is not clear why this protein would be both myristylated and palmitylated. Only class four palmitylproteins, such as the Src family of proteins, have been shown to be both myristylated and palmitylated. The A-type inclusion protein expressed by cowpox virus forms a large symmetrical matix in the cytoplasm of infected cells and generally contains mature virions. It is possible, therefore, that the function of acylation may be to stabilize the protein matrix or to assist in occlusion of enveloped virus particles.
Resource Type
Date Available
Date Copyright
Date Issued
Degree Level
Degree Name
Degree Field
Degree Grantor
Commencement Year
Advisor
Committee Member
Non-Academic Affiliation
Subject
Rights Statement
Peer Reviewed
Language
Digitization Specifications
  • File scanned at 300 ppi (Monochrome, 256 Grayscale) using Capture Perfect 3.0 on a Canon DR-9050C in PDF format. CVista PdfCompressor 4.0 was used for pdf compression and textual OCR.
Replaces
Additional Information
  • description.provenance : Approved for entry into archive by Patricia Black(patricia.black@oregonstate.edu) on 2012-10-01T18:52:11Z (GMT) No. of bitstreams: 1 MartinKarenH1998.pdf: 22320746 bytes, checksum: ee52bc39d3ba691285c79ccc2e4b4aea (MD5)
  • description.provenance : Made available in DSpace on 2012-10-01T18:53:04Z (GMT). No. of bitstreams: 1 MartinKarenH1998.pdf: 22320746 bytes, checksum: ee52bc39d3ba691285c79ccc2e4b4aea (MD5) Previous issue date: 1997-04-21
  • description.provenance : Submitted by Erin Clark (ecscannerosu@gmail.com) on 2012-10-01T18:04:28Z No. of bitstreams: 1 MartinKarenH1998.pdf: 22320746 bytes, checksum: ee52bc39d3ba691285c79ccc2e4b4aea (MD5)
  • description.provenance : Approved for entry into archive by Patricia Black(patricia.black@oregonstate.edu) on 2012-10-01T18:53:04Z (GMT) No. of bitstreams: 1 MartinKarenH1998.pdf: 22320746 bytes, checksum: ee52bc39d3ba691285c79ccc2e4b4aea (MD5)

Relationships

In Administrative Set:
Last modified: 08/09/2017

Downloadable Content

Download PDF
Citations:

EndNote | Zotero | Mendeley

Items