Header Logo

Search Result Details

This page shows the details of why an item matched the keywords from your search.
One or more keywords matched the following properties of Morrison, Trudy
PropertyValue
overview

Academic Background

B.A. Wellesley College
Ph. D.Tufts University School of Medicine
Postdoctoral training at Massachusetts Institute of Technology

Dr. Trudy Morrison

Mechanisms of Paramyxovirus Membrane Fusion
Assembly of Paramyxoviruses
Development of Virus Vaccines

My laboratory is exploring the molecular mechanisms of paramyxovirus entry into susceptible cells and the assembly and release of infectious virus from infected cells. Paramyxoviruses are simple negative-stranded, enveloped RNA viruses. The two viral glycoproteins, the hemagglutinin-neuraminidase (HN) protein and the fusion (F) protein, mediate entry of the virus into cells. The HN protein is the virus attachment protein and the F protein directly mediates the membrane fusion required for virus penetration. However, the HN protein is required to activate the fusion activity of the F protein. Using Newcastle disease virus as a model paramyxovirus, my laboratory is exploring the molecular mechanisms involved in the activation of the fusion protein and the requirements for the conformational changes in the F protein required to mediate membrane fusion.

Release of progeny paramyxoviruses from infected cells requires the assembly of the structural components of the virion, the viral glycoproteins, the matrix protein, and the ribonucleoprotein core, followed by the budding of mature virus from surfaces of infected cells. We are exploring the protein interactions required for the formation of assembly complexes, the cell domains involved in virus assembly, and the host cell contributions to virus assembly and release.

My laboratory is also exploring the potential of virus-like particles as vaccines for different paramyxoviruses.

One or more keywords matched the following items that are connected to Morrison, Trudy
Item TypeName
Academic Article Assembly of viral membranes. I. Association of vesicular stomatitis virus membrane proteins and membranes in a cell-free system.
Academic Article Disulfide bond formation is a determinant of glycosylation site usage in the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus.
Academic Article Assembly of viral membranes: maturation of the vesicular stomatitis virus glycoprotein in the presence of tunicamycin.
Academic Article Incorporation of functional HN-F glycoprotein-containing complexes into newcastle disease virus is dependent on cholesterol and membrane lipid raft integrity.
Academic Article Assembly of viral membranes: nature of the association of vesicular stomatitis virus proteins to membranes.
Academic Article Conformational change in a viral glycoprotein during maturation due to disulfide bond disruption.
Academic Article Mutational changes in the vesicular stomatitis virus glycoprotein affect the requirement of carbohydrate in morphogenesis.
Academic Article Characterization of the soluble glycoprotein released from vesicular stomatitis virus-infected cells.
Academic Article Fatty acid modification of Newcastle disease virus glycoproteins.
Academic Article Synthesis, stability, and cleavage of Newcastle disease virus glycoproteins in the absence of glycosylation.
Academic Article Conformationally sensitive antigenic determinants on the HN glycoprotein of Newcastle disease virus form with different kinetics.
Academic Article Structure and assembly of a paramyxovirus matrix protein.
Academic Article Long-term and memory immune responses in mice against Newcastle disease virus-like particles containing respiratory syncytial virus glycoprotein ectodomains.
Academic Article Intracellular processing of the vesicular stomatitis virus glycoprotein and the Newcastle disease virus hemagglutinin-neuraminidase glycoprotein.
Academic Article The role of individual oligosaccharide chains in the activities of the HN glycoprotein of Newcastle disease virus.
Academic Article Mutations in the cytoplasmic domain of the fusion glycoprotein of Newcastle disease virus depress syncytia formation.
Concept Glycoproteins
Academic Article Newcastle disease virus-like particles: preparation, purification, quantification, and incorporation of foreign glycoproteins.
Academic Article Alternative Virus-Like Particle-Associated Prefusion F Proteins as Maternal Vaccines for Respiratory Syncytial Virus.
Academic Article The Respiratory Syncytial Virus (RSV) G Protein Enhances the Immune Responses to the RSV F Protein in an Enveloped Virus-Like Particle Vaccine Candidate.
Search Criteria
  • Glycoproteins