Susan Hafenstein Department of Medicine, Pennsylvania State University College USA

Susan Hafenstein

Department of Medicine, Pennsylvania State University College of Medicine, USA

Research fields

Microbiology

Personal information

Education

Ph.D. in Pathobiology, University of Arizona, Tucson, AZ, 2003

Current position

Assistant Professor in Medicine (Infectious Diseases) and Microbiology and Immunology, Pennsylvania State University College of Medicine, Hershey, PA (2009-to date)

Publications

Fifteen most pertinent peer-reviewed publications (15 of 31)

Lee, H., Cifuente, J. O., Ashley, R. E., Conway, J. F., Makhov, A. M., Tano, Y., Shimizu, H., Nishimura, Y. and Hafenstein, S. (2013). A strain-specific epitope of enterovirus 71 identified by cryo-electron microscopy of the complex with fab from neutralizing antibody. J Virol 87(21): 11363-11370.
Nishimura, Y., Lee, H., Hafenstein, S., Kataoka, C., Wakita, T., Bergelson, J. M. and Shimizu, H. (2013). Enterovirus 71 binding to PSGL-1 on leukocytes: VP1-145 acts as a molecular switch to control receptor interaction. PLoS Pathog 9(7): e1003511.
Cifuente, J. O., Lee, H., Yoder, J. D., Shingler, K. L., Carnegie, M. S., Yoder, J. L., Ashley, R. E., Makhov, A. M., Conway, J. F. and Hafenstein, S. (2013). Structures of the procapsid and mature virion of enterovirus 71 strain 1095. J Virol 87(13): 7637-7645.
Shingler, K. L., Yoder, J. L., Carnegie, M. S., Ashley, R. E., Makhov, A. M., Conway, J. F. and Hafenstein, S. (2013). The enterovirus 71 A-particle forms a gateway to allow genome release: a cryoEM study of picornavirus uncoating. PLoS Pathog 9(3): e1003240.
Yoder, J. D., Cifuente, J. O., Pan, J., Bergelson, J. M. and Hafenstein, S. (2012). The crystal structure of a coxsackievirus B3-RD variant and a refined 9-angstrom cryo-electron microscopy reconstruction of the virus complexed with decay-accelerating factor (DAF) provide a new footprint of DAF on the virus surface. J Virol 86(23): 12571-12581.
Stucker, K. M., Pagan, I., Cifuente, J. O., Kaelber, J. T., Lillie, T. D., Hafenstein, S., Holmes, E. C. and Parrish, C. R. (2012). The role of evolutionary intermediates in the host adaptation of canine parvovirus. J Virol 86(3): 1514-1521.
Ning, X., Nguyen, D., Mentzer, L., Adams, C., Lee, H., Ashley, R., Hafenstein, S. and Hu, J. (2011). Secretion of genome-free hepatitis B virus--single strand blocking model for virion morphogenesis of para-retrovirus. PLoS Pathog 7(9): e1002255.
Pan, J., Narayanan, B., Shah, S., Yoder, J. D., Cifuente, J. O., Hafenstein, S. and Bergelson, J. M. (2011). Single amino acid changes in the virus capsid permit coxsackievirus B3 to bind decay-accelerating factor. J Virol 85(14): 7436-7443.
Plevka, P.*, Hafenstein, S.*, Harris, K. G., Cifuente, J. O., Zhang, Y., Bowman, V. D., Chipman, P. R., Bator, C. M., Lin, F., Medof, M. E. and Rossmann, M. G. (2010). Interaction of decay-accelerating factor with echovirus 7. J Virol 84(24): 12665-12674. *Shared first authorship
Goodman, L. B., Lyi, S. M., Johnson, N. C., Cifuente, J. O., Hafenstein, S. L. and Parrish, C. R. (2010). Binding site on the transferrin receptor for the parvovirus capsid and effects of altered affinity on cell uptake and infection. J Virol 84(10): 4969-4978.
Hafenstein, S., Bowman, V. D., Sun, T., Nelson, C. D., Palermo, L. M., Chipman, P. R., Battisti, A. J., Parrish, C. R. and Rossmann, M. G. (2009). Structural comparison of different antibodies interacting with parvovirus capsids. J Virol 83(11): 5556-5566.
Hafenstein, S., Bowman, V. D., Chipman, P. R., Bator Kelly, C. M., Lin, F., Medof, M. E. and Rossmann, M. G. (2007). Interaction of decay-accelerating factor with coxsackievirus B3. J Virol 81(23): 12927-12935.
Hafenstein, S., Palermo, L. M., Kostyuchenko, V. A., Xiao, C., Morais, M. C., Nelson, C. D., Bowman, V. D., Battisti, A. J., Chipman, P. R., Parrish, C. R. and Rossmann, M. G. (2007). Asymmetric binding of transferrin receptor to parvovirus capsids. Proc Natl Acad Sci U S A 104(16): 6585-6589.
Hafenstein, S. L., Chen, M. and Fane, B. A. (2004). Genetic and functional analyses of the oX174 DNA binding protein: the effects of substitutions for amino acid residues that spatially organize the two DNA binding domains. Virology 318(1): 204-213.
Hafenstein, S. and Fane, B. A. (2002). phi X174 genome-capsid interactions influence the biophysical properties of the virion: evidence for a scaffolding-like function for the genome during the final stages of morphogenesis. J Virol 76(11): 5350-5356.