Trudy Morrison, Ph.D.

Academic Role: Professor

Faculty Appointment(s) In:
   Molecular Genetics and Microbiology

Other Affiliation(s):
   Center for AIDS Research
   Program in Immunology and Virology

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.

Representative Publications

Morrison T.  Structure and Function of a Paramyxovirus Fusion Protein  2003  Biochimica et Biophysica Acta:  1614:  73-84.

Dolganiuc, V., McGinnes, L., Luna, E., and Morrison, T. 2003 The role of the cytoplasmic domain of the Newcastle disease virus Fusion protein in association with lipid rafts.  J. Virol. 77:  12968-12979

McGinnes, L., Pantua, H., Reitter, J., and Morrison, T.  2005  Purification and propagation of Newcastle disease virus.  Current Protocols in Microbiology.

Pantua, H., McGinnes, L. W., Leszyk, J., and Morrison, T.  2005.  Characterization of an alternate form of the NDV Fusion protein.  J. Virol.  79:  11660-11670

McGinnes, L, and Morrison, T.  2006  Inhibition of receptor binding stabilizes Newcastle disease virus HN and F protein containing complexes.  J. Virol. 80:  2894-2903

Laliberte, J, P., McGinnes, L. W., Peeples, M. E., and Morrison, T. G.  2006 Integrity of membrane lipid rafts is necessary for the ordered assembly and release of infectious Newcastle disease virus particles.  J. Virol. 80:  10652-10662

Pantua, H. D., McGinnes, L. W., Peeples, M. E., and Morrison, T. G. 2006 Requirements for the assembly and release of Newcastle disease virus-like particles.  J. Virol. 80:  11062-11-73.

Jain, S, McGinnes, L, and Morrison, T.  2007.  Thiol/disulfide exchange is required for membrane fusion directed by the Newcastle disease virus Fusion protein.  J. Virol. 81:  2328-2339.

Laliberte, J., McGinnes, L., and Morrison, T.  2007.  Incorporation of functional HN-F glycoprotein-containing complexes into Newcastle disease virus is dependent on cholesterol and membrane lipid raft integrity.  J. Virol. 81:  10636-10648.

Academic Background

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

Office: S5-250
Phone: 508-856-6592
E-mail: Trudy.Morrison@umassmed.edu
Keywords: Intracellular Trafficking, Cell Biology, Virology

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