Email: Office Phone: 318-675-5760
Laboratory Phone: 318-675-5761
Office Fax: 318-675-5764
Postdoctoral Study, University of Rochester
Ph.D., Molecular Genetics, 1987 University of Konstanz
M.S. (Diplom), Molecular Genetics, 1984, University of Konstanz
B.S. (Vordiplom), Biology, 1981, University of Konstanz
Major Research Interests: Virus cell interactions, molecular pathogenesis of oncogenic human papillomaviruses
Certain types of human papillomaviruses (HPV) are the major cause of virus-induced malignancies in the human, like cervical carcinoma, the second most common cancer in women worldwide. Papillomaviruses are non-enveloped DNA viruses which exclusively replicate in the skin and mucosa. Due to the dependence on terminally differentiating tissues for their propagation, the study of the papillomavirus life cycle has been hampered. The development of surrogate systems for the generation of papillomaviruses in recent years has now opened ways to investigate processes involved in virus binding, uptake, and intracellular transport as well as the assembly of progeny virus. We are specifically interested in identifying cellular factors functioning as papillomavirus receptors, in the study of virus uptake and intracellular transport, in the analysis of the uncoating process, and the passing of cellular membranes by the virus genome. In addition, we are also studying innate immune defences employed by the host cells to fight off HPV infection.
Florin, L., Becker, K.A., Sapp, C., Lambert, C., Sirma, H., Müller, M., Streeck, R.E., and Sapp, M. (2004): Nuclear translocation of papillomavirus minor capsid protein L2 requires Hsc70. J. Virol. 78:5546-5553.
Kämper, N., Day, P. M., Nowak, T., Selinka, H.-C., Florin, L., Bolscher, J. G., Hilbig, L., Schiller, J. T., and Sapp, M. (2006): A membrane-destabilizing peptide in capsid protein L2 required for egress of papillomavirus genomes from endosomes. J. Virol. 80:759-768.
Florin, L., Becker, K. A., Lambert, C., Nowak, T., Sapp, C., Strand, D., Streeck, R. E., and Sapp, M. (2006): Identification of a dynein interacting domain in the papillomavirus minor capsid protein L2. J. Virol. 80:6691-6696.
Knappe, M., Bodevin, S., Selinka, H.-C., Spillmann, D., Streeck, R. E., Chen, X., Lindahl, U., and Sapp, M. (2007): Surface-exposed amino acids of HPV16 L1 protein mediating interaction with cell surface heparan sulphate. J. Biol. Chem.: 282:27913-29222.
Selinka, H.-C., Florin, L., Patel, H.D., Freitag, K., Schmidtke, M., Makarov, V.A., Sapp, M. (2007): Inhibition of transfer to secondary receptors by heparan sulfate-binding drug or antibody induces non-infectious uptake of human papillomavirus. J. Virol. 81: 10970-10980.
Spoden, G., Freitag, K., Husmann, M., Boller, K., Sapp, M., Lambert, C., and Florin, L. (2008): Clathrin- and caveolin-independent entry of human papillomavirus type 16 – involvement of tetraspanin enriched microdomains (TEMs). PLoS ONE 3(10):e3313.
Bienkowska-Haba, M., Patel, H.D., and Sapp, M. (2009): Target cell cyclophilins facilitate human papillomavirus type 16 infection. PLoS Pathog. 5(7):e1000524.
Dasgupta J, Bienkowska-Haba M, Ortega ME, Patel HD, Bodevin S, Spillmann D, Bishop B, Sapp M, Chen XS. Structural basis of oligosaccharide receptor recognition by human Papillomavirus. J Biol Chem. 2011 Jan 28. 286(4):2617-24. Epub 2010 Nov 29.
All Publications: PubMed