Current Research

The Hardy laboratory studies interactions between enteric viruses and host cells at the molecular level. We seek to understand how protein-protein interaction networks regulate both viral gene expression and the host cell genetic response to virus invasion. Research in the lab focuses on the rotaviruses, the most important cause of pediatric diarrhea worldwide. Current projects in the lab include molecular and proteomic investigations of how rotaviruses modulate cellular antiviral gene expression, and mechanisms of innate immunity to viral infection.

Recent Publications

Ettayebi, K. and M.E. Hardy 2003. The Norwalk virus nonstructural protein p48 binds the SNARE-regulator VAP-A and disrupts secretory vesicle trafficking. J. Virol. 77: 11790-11797.

Lochridge, V. P., K. Jutila, J. W. Graff, and M. E. Hardy. 2005. Epitopes in the P2 domain of norovirus VP1 involved in virus-host cell interactions. J. Gen Virol: 86: 2799

Hardy, M.E. 2005. Norovirus protein structure and function. FEMS Microbiol Lett 253 (1):1-8

Buckner, D., S. Wilson, S. Kurk, M.E Hardy, and M.A. Jutila. 2006. Use of early passage fetal intestinal epithelial cells in semi-high-throughput screening assays: An approach to identify new innate immune system adjuvants. J Biomol Screen Sep;11(6):664-71.

Shaneyfelt, M.E., Burke, A.D., Graff, J.W., Jutila, M.A. and M.E. Hardy. 2006 Natural products that reduce rotavirus infectivity identified by a chemiluminescent moderate throughput assay. Virology J 3:68.

Daughenbaugh, K., C. Wobus and M.E. Hardy. 2006 Murine norovirus VPg binds eIFs in infected cells. Virology J 3:33.

Graff J.W., J. Ewen, K. Ettayebi, and M.E. Hardy. 2007. The zinc binding domain of rotavirus NSP1 is required for proteasome-dependent degradation of IRF3. J Gen Virol 88:613-20.

Lochridge, V.P. and M.E. Hardy. 2007. A single amino acid substitution in the P2 domain of VP1 is sufficient for escape from antibody neutralization. J Virol 81: 12316-12322.

Ettayebi, K and M.E. Hardy. 2008. Recombinant norovirus-specific scFv inhibit virus-like particle binding to cellular ligands. Virology J 5:21.

Graff, J.W., K Ettayebi and M.E. Hardy Rotavirus NSP1 inhibits NFκB activation by targeting β-TrCP for degradation: a novel mechanism of IFN antagonism. In revision