Martin I. Muggeridge, Ph.D.

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 and Epstein-Barr 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. Epstein-Barr virus (EBV) causes infectious mononucleosis and plays an important role in the development of several B cell and epithelial cell cancers. Like other herpesviruses, both have a lipid envelope containing many membrane proteins, and their entry into cells, and for HSV-2 its subsequent spread to adjacent cells, requires membrane fusion. Transient coexpression of HSV-2 membrane proteins gB, gD, gH and gL, or EBV proteins gB, gH and gL, causes cell fusion in the absence of infection, in a process that in many respects mimics fusion between the virus and cell membranes. Three-dimensional structures are known for gB and the gH/gL complex of both viruses, and there is some limited information from mutagenesis studies about which residues lie within functionally important parts of the proteins. The activity of gB in fusion is generally believed to be triggered by an interaction with gH/gL, but the location of the binding sites on either protein is not clear. Determination of the binding site on gB may facilitate the design of drugs able to interfere with the interaction and thus block membrane fusion and virus entry into cells. This is the current focus of the lab.

Representative Publications:

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.

J. Legoff, H. Bouhlal, M. Lecerf, C. Klein, H. Hocini, A. Si-Mohamed, M.I. Muggeridge, and L. Bélec. 2007. HSV-2- and HIV-1-permissive cell lines co-infected by HSV-2 and HIV-1 co-replicate HSV-2 and HIV-1 without production of HSV-2/HIV-1 pseudotype particles. Virology Journal 4, 1-10.

Muggeridge, M.I.. 2012. Glycoprotein B of herpes simplex virus 2 has more than one intracellular conformation and is altered by low pH. J. Virol. 86, 6444-6456.

All Publications: PubMed