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Search Results to Trudy G Morrison PhD

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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 Role of cotranslational disulfide bond formation in the folding of the hemagglutinin-neuraminidase protein of Newcastle disease virus.
Academic Article Disulfide bond formation is a determinant of glycosylation site usage in the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus.
Academic Article The three faces of paramyxovirus attachment proteins.
Academic Article Avian cells expressing the Newcastle disease virus hemagglutinin-neuraminidase protein are resistant to Newcastle disease virus infection.
Academic Article Fatty acid modification of Newcastle disease virus glycoproteins.
Academic Article The fusion promotion activity of the NDV HN protein does not correlate with neuraminidase activity.
Academic Article Retroviral expressed hemagglutinin-neuraminidase protein protects chickens from Newcastle disease virus induced disease.
Academic Article Aberrant membrane insertion of a cytoplasmic tail deletion mutant of the hemagglutinin-neuraminidase glycoprotein of Newcastle disease virus.
Academic Article Nucleotide sequence of the gene encoding the Newcastle disease virus hemagglutinin-neuraminidase protein and comparisons of paramyxovirus hemagglutinin-neuraminidase protein sequences.
Academic Article Intracellular processing of the vesicular stomatitis virus glycoprotein and the Newcastle disease virus hemagglutinin-neuraminidase glycoprotein.
Academic Article The attachment function of the Newcastle disease virus hemagglutinin-neuraminidase protein can be separated from fusion promotion by mutation.
Concept Neuraminidase

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  • Neuraminidase