Associate Professor

Contact Information:
Email: mmugge@lsuhsc.edu
Office Phone: 318-675-7571
Laboratory Phone: 318-675-7572
Office Fax: 318-675-5764

Education/Training:
Research Assistant Professor, University of Pennsylvania School of Dental Medicine
Postdoctoral Study, Wistar Institute of Anatomy and Biology
Ph.D., Virology, 1983, University of London/National Institute for Medical Research
M.A., Biochemistry, 1983, University of Oxford
B.A., Biochemistry, 1979, University of Oxford

Major Research Interests:
Herpes simplex virus membrane proteins; virus entry; membrane fusion; membrane protein trafficking.

Herpes simplex virus 2 (HSV-2) causes recurrent genital infections and life-threatening neonatal disease. Like other herpesviruses, it has a lipid envelope containing many membrane proteins. Entry of HSV-2 into cells, its subsequent spread to adjacent cells, and its ability to cause cell fusion, all require membrane fusion. Transient coexpression of four viral membrane proteins (gB, gD, gH and gL) causes cell fusion in the absence of infection, and mutations in the cytoplasmic tail of gB increase the extent of fusion in this assay and when cells are infected with viruses carrying such mutations. The scarcity of these mutations in clinical isolates of HSV-2 suggests that excessive fusion is deleterious to the virus in vivo, and that fusion may be a regulated process. The cytoplasmic tail of gB also contains a number of potential trafficking signals, at least one of which is involved in endocytosis of gB from the plasma membrane via an interaction with the AP-2 adaptor complex. Several additional cell proteins that are involved directly or indirectly with cell membrane protein trafficking interact with the cytoplasmic tail, and may be involved in intracellular trafficking of gB.

Representative Publications:
Cockrell, A. S. and M. I. Muggeridge. 1998. Herpes simplex virus 2 UL45 is a type II membrane protein. J. Virol. 72:4430-4433.

Norton, D. D., D. Dwyer and M. I. Muggeridge. 1998. Use of a neural network secondary structure prediction to define targets for mutagenesis of herpes simplex virus glycoprotein B. Virus Res. 55:37-48.

J. C . Whitbeck, M. I. Muggeridge, A. H. Rux, W. Hou, C. Krummenacher, H. Lou, A. van Geelen, R. J. Eisenberg and G. H. Cohen. 1999. The major neutralizing antigenic site on herpes simplex virus glycoprotein D overlaps a receptor-binding domain. J. Virol. 73:9879-9890.

Muggeridge, M. I. 2000. Characterization of cell-cell fusion mediated by herpes simplex virus 2 glycoproteins gB, gD, gH and gL in transfected cells. J. Gen. Virol. 81:2017-2027.

Fan, Z. H., M. L. Grantham, M. S. Smith, E. A. Anderson, J. A. Cardelli, and M. I. Muggeridge. 2002. Truncation of herpes simplex virus type 2 glycoprotein B increases its cell surface expression and activity in cell-cell fusion, but these properties are unrelated. J. Virol. 76:9271-9283.

Muggeridge, M. I., M. L. Grantham, and F. B. Johnson. 2004. Identification of syncytial mutations in a clinical isolate of herpes simplex virus 2 . Virology 328:244-253.

W. Li, T. J. Minova-Foster, D. D. Norton, and M. I. Muggeridge. (2006). Identification of functional domains in herpes simplex virus 2 glycoprotein B . J. Virol. 80, 3792-3800.