Gary Whittaker, PhD
Dr. Whittaker's FIP research is highlighted in the video here: https://research.cornell.edu/video/veterinary-college-breakthrough-uncovers-key-fighting-deadliest-cat-virus-video
In collaboration with the lab of David Putnum (Dept. Biomedical Engineering) we are evaluating novel vaccine platforms for influenza virus, as well as investigating novel therapeutic options for influenza and paramyxoviruses that target host cell proteases. Our work on influenza also covers the risk assessment aspects of emerging human and avian influenza viruses, in association with single-particle imaging in the laboratory of Susan Daniel (School of Chemical Engineering).
Coronaviruses are major cause of disease in many animal species and have become increasingly important as human pathogens. Our studies are focused on a structure-function analysis of the viral spike (S) and its role in virus entry and membrane fusion. We study both receptor interactions as well as how proteases activate S, and how mutations in the viral genome allow selection of distinct proteases allowing increased pathogenesis. Our studies include work on Middle East Respiratory Syndrome (MERS) coronavirus under BSL3 conditions, feline coronaviruses, canine coronavirus, and emerging coronaviruses of pigs (PEDV) and horses (EqCoV).
Rhabdoviruses includes many important human, animal and plant pathogens, including Rabies virus. Vesicular stomatitis virus (VSV) is a prototypic virus in the Rhabdoviridae, and it is a focus of the Whittaker Lab. Using the information provided by the recent crystal structure of the VSV glycoprotein (G), we are carrying out a mutagenesis study to determine the critical amino acids within the fusion domain of VSV G, as well as a related fish rhabdovirus, viral hemorrhagic septicemia virus (VHSV).
Ebola virus, along with the related Marburg virus, are filoviruses that are currently of high significance in public health. Our studies are focused on the structure-function relationship of the viral glycoprotein (GP; its role in virus entry and membrane fusion and the potential for development of new anti-viral therapeutics targeting virus fusion. This work is in collaboration with Dr. Susan Daniel (School of Chemical and Bimolecular Engineering). We study the virus as non-replicating pseudovirons, using single particle imaging, TIRF microscopy and supported lipid bilayers. Our studies also include work on the host cell proteases activating Ebola and Marburg virus GP.
Ph.D. (University of Leeds, UK)
Dr. Whittaker is a Professor in the Department of Microbiology and Immunology and has been associated with the department since 1996. He received a bachelor's degree in Biochemistry and his Ph.D. in Microbiology from Leeds University U.K. where he studied the molecular biology and biochemistry of equine herpesvirus. He obtained postdoctoral training at Yale University in the laboratory of Dr. Ari Helenius, studying the cell biology of influenza virus replication. Dr Whittaker's laboratory is focused on the entry of influenza viruses, rhaboviurses and coronaviruses into host cells and is funded by research grants from the National Institutes of Health.
André, N.M., Cossec, B., Davies, E., Miller A.D. and Whittaker G.R. (2019). Distinct mutation in the feline coronavirus spike protein cleavage-activation site in a cat with feline infectious peritonitis-associated meningoencephalomyelitis. J. Feline Med. Surg. Open Reports 5: 1, June 26, 2019.
Jaimes, J.A. and Whittaker G.R. (2018). Feline coronavirus: Insights into viral pathogenesis based on the spike protein structure and function. Virology 517:108-121.
Lai, A.L., Millet, J.K., Daniel, S. Freed, J.H, and Whittaker, G.R. (2017). The SARS-CoV fusion peptide forms an extended bipartite fusion platform that perturbs membrane order in a calcium-dependent manner. J. Mol. Biol. 429(24):3875-3892.
Watkins, H.C., Rappazzo, C.G., Higgins, J.S., Sun, X., Brock, N., Chau, A., Misra, A., Cannizzo, J.P., King, M.R., Maines, T.R., Leifer, C.A, Whittaker, G.R., DeLisa, M.P. and Putnam, D. (2017). Safe recombinant outer membrane vesicles that display M2e elicit heterologous influenza protection. Mol. Ther. 25:989-1002.
Millet, J.K. and Whittaker, G.R. (2014).Host cell entry of Middle East respiratory syndrome coronavirus following two-step, furin-mediated activation of spike protein. Proc. Natl. Acad. Sci. USA. 111: 15214-15219.
Licitra, B.N., Millet, J.K, Regan, A.D., Hamilton, B.S., Rinaldi, V., Duhamel, G.E. and Whittaker G.R. (2013). Mutation in spike protein cleavage site and pathogenesis of feline coronavirus. Emerg. Infect. Dis. 19: 1066-1073.
Tse, L.V., Marcano, V.C., Huang. W., Pocwierz, M.S. and Whittaker, G.R. (2013). Plasmin-mediated activation of pandemic H1N1 influenza virus hemagglutinin independent of the viral neuraminidase. J. Virol. 87: 5161-5169
Licitra, B.N., Sams, K.L. Lee, D.W. and Whittaker G.R. (2014). Feline coronaviruses associated with feline infectious peritonitis have modifications to spike protein activation sites at two discrete positions. ArXiV.http://arxiv.org/abs/1412.4034.
Costello, D.A., Whittaker, G.R. and Daniel, S. (2015).Variation of pH sensitivity, acid stability, and fusogenicity of three influenza H3 subtypes. J. Virol. 89(1):350-360.http://www.ncbi.nlm.nih.gov/pubmed/25320308.
Millet, J.K. and Whittaker, G.R. Host cell entry of Middle East respiratory syndrome coronavirus following two-step, furin-mediated activation of spike protein. Proc Natl Acad Sci.:http://www.pnas.org/content/early/2014/10/02/1407087111.abstract
Hamilton, B.S., Chung, C., Cyphers, S., Rinaldi, V.D., Marcano, V., and Whittaker, G.R., (2014). Inhibition of influenza virus infection and hemagglutinin cleavage by the protrease inhibitor HAI-2. Biochem. Biophys. Res. Commun. 2014 Jun 27.http://www.sciencedirect.com/science/article/pii/S0006291X14011838
Belouzard, S. Chu, V.C. and Whittaker G.R. (2009).Activation of the severe acute respiratory syndrome coronavirus (SARS-CoV) spike protein via sequential proteolytic cleavage at two distinct sites. Proc Natl Acad Sci U S A. 2009 Mar 24. [Epub ahead of print] PMID: 19321428 Full Text Available
Awards and Honors