The Resource Characterizing the retroviral envelope glycoprotein membrane proximal external region and membrane-spanning domains for their roles in helical alignment, fusogenicity, and incorporation into viral particles, By Daniel Salamango

Characterizing the retroviral envelope glycoprotein membrane proximal external region and membrane-spanning domains for their roles in helical alignment, fusogenicity, and incorporation into viral particles, By Daniel Salamango

Label
Characterizing the retroviral envelope glycoprotein membrane proximal external region and membrane-spanning domains for their roles in helical alignment, fusogenicity, and incorporation into viral particles
Title
Characterizing the retroviral envelope glycoprotein membrane proximal external region and membrane-spanning domains for their roles in helical alignment, fusogenicity, and incorporation into viral particles
Statement of responsibility
By Daniel Salamango
Creator
Contributor
Author
Thesis advisor
Subject
Genre
Language
eng
Summary
Retroviruses readily form pseudotyped particles with a diverse panel of viral glycoproteins from similar and unrelated families. This phenomenon has been exploited by researchers from various fields for manipulation of retroviral vectors to target specific cell types. One limitation, however, is that very little is known about the pseudotyping mechanism. If we can gain insight into the molecular mechanism of this process, then potentially non-viral surface proteins could be engineered to incorporate into viral particles. This could greatly broaden the range of cell types that could be specifically targeted by lentiviral gene delivery vectors. My work has shown that the MSD of MLV Env has critical protein components necessary for fusogenicity and that the MPER and MSD both contribute to MLV Env incorporation into viral particles. Additionally, my work provided insight into the ability for the viral Env protein to accomplish viral-to-cell membrane fusion. I identified four hydroxyl-containing residues at the C-terminus of the MPER and Nterminus of the MSD that are critical for Env fusogenicity. Further study revealed that these residues may be part of a SxxxTTxxS motif previously observed to influence oligomerization of membrane helices. Interestingly, other gamma-retroviral glycoproteins such as FLV and GaLV Env also have this serine/threonine clustering. The same motif can also be found in VSV-G and in many different strains of the influenza virus, both A and B. It is plausible that this motif has an evolutionary advantage to aide in regulation of fusogenic activity
Cataloging source
MUU
http://library.link/vocab/creatorDate
1987-
http://library.link/vocab/creatorName
Salamango, Daniel
Degree
PhD
Dissertation note
Thesis
Dissertation year
2015.
Government publication
government publication of a state province territory dependency etc
Granting institution
University of Missouri--Columbia
Illustrations
illustrations
Index
no index present
Literary form
non fiction
Nature of contents
  • dictionaries
  • bibliography
  • theses
http://library.link/vocab/relatedWorkOrContributorName
Johnson, Marc
http://library.link/vocab/subjectName
  • Retroviruses
  • Glycoproteins
  • Viral envelopes
  • Membrane fusion
Label
Characterizing the retroviral envelope glycoprotein membrane proximal external region and membrane-spanning domains for their roles in helical alignment, fusogenicity, and incorporation into viral particles, By Daniel Salamango
Instantiates
Publication
Note
  • Includes vita
  • Abstract from short.pdf
  • "A dissertation presented to the Faculty of the Graduate School at the University of Missouri-Columbia In Partial Fulfillment Of the Requirements for the Degree Doctor of Philosophy."
  • Dissertation supervisor: Dr. Marc C. Johnson
Bibliography note
Includes bibliographical references (pages 237-273)
Carrier category
online resource
Carrier category code
cr
Carrier MARC source
rdacarrier
Content category
text
Content type code
txt
Content type MARC source
rdacontent
Control code
957559420
Extent
1 online resource (viii, 274 pages)
Form of item
online
Media category
computer
Media MARC source
rdamedia
Media type code
c
Other physical details
illustrations (some color)
Specific material designation
remote
System control number
(OCoLC)957559420
Label
Characterizing the retroviral envelope glycoprotein membrane proximal external region and membrane-spanning domains for their roles in helical alignment, fusogenicity, and incorporation into viral particles, By Daniel Salamango
Publication
Note
  • Includes vita
  • Abstract from short.pdf
  • "A dissertation presented to the Faculty of the Graduate School at the University of Missouri-Columbia In Partial Fulfillment Of the Requirements for the Degree Doctor of Philosophy."
  • Dissertation supervisor: Dr. Marc C. Johnson
Bibliography note
Includes bibliographical references (pages 237-273)
Carrier category
online resource
Carrier category code
cr
Carrier MARC source
rdacarrier
Content category
text
Content type code
txt
Content type MARC source
rdacontent
Control code
957559420
Extent
1 online resource (viii, 274 pages)
Form of item
online
Media category
computer
Media MARC source
rdamedia
Media type code
c
Other physical details
illustrations (some color)
Specific material designation
remote
System control number
(OCoLC)957559420

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