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Title page for ETD etd-11282005-150051

Type of Document Dissertation
Author Campbell, Jacquelyn Andrea
Author's Email Address jackie.campbell@vanderbilt.edu
URN etd-11282005-150051
Title Structure-function analysis of reovirus binding to junctional adhesion molecule-A
Degree PhD
Department Microbiology and Immunology
Advisory Committee
Advisor Name Title
Earl Ruley Committee Chair
James Crowe Committee Member
Luc Van Kaer Committee Member
Phoebe Stewart Committee Member
Richard Hoover Committee Member
Terence S. Dermody Committee Member
  • zo-1
  • junctional adhesion molecule
  • reovirus
  • tight junction
Date of Defense 2005-09-23
Availability unrestricted
Mammalian reoviruses are nonenveloped, double-stranded RNA viruses that serve as important models for studies of viral neuropathogenesis. Reovirus disease is initiated by binding of the virus to receptors on the surface of target cells. We identified junctional adhesion molecule-A (JAM-A), a tight junction protein, as a receptor for reovirus. Using a structure-function analysis we identified sequences in virus and receptor required for productive infection. Reovirus engagement of JAM-A in polarized epithelial cells during the entry phase induces a redistribution of JAM-A-associated proteins and increases paracellular permeability. The discovery that reovirus-JAM-A interactions alter tight junction integrity expands our knowledge of the physiologic effects of virus-receptor interactions and highlights a potential role for the tight junction in regulating the cellular response to viral infection.
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