Ileana M. Cristea

Ileana Cristea is a Professor in the Department of Molecular Biology at Princeton University. Her laboratory focuses on characterizing mechanisms of cellular defense against viruses, as well as mechanisms used by viruses to manipulate these critical cellular processes. Towards these goals, she has promoted the integration of virology with proteomics and bioinformatics. She has developed methods for studying virus-host protein interactions in space and time during the progression of an infection, which have allowed her group to bridge developments in mass spectrometry to important findings in virology. For example, her laboratory has contributed to the emergence of the research field of nuclear DNA sensing in immune response, and has discovered sirtuins as broad-spectrum antiviral factors. Dr. Cristea is the President elect of US HUPO, chairs the Infectious Disease initiative of the Human Proteome World Organization, and has acted on the Education Committee of the American Society for Mass Spectrometry. She has taught the Proteomics Course at Cold Spring Harbor Laboratory for over ten years, and is Senior Editor for mSystems, and on the Editorial Boards of Molecular Systems Biology and Molecular & Cellular Proteomics. She was recognized with the Bordoli Prize from the British Mass Spectrometry Society (2001), NIDA Avant-Garde Director Pioneer Award for HIV/AIDS Research (2008), Human Frontiers Science Program Young Investigator Award (2009), Early Career Award in Mass Spectrometry from the American Chemical Society (2011), the American Society for Mass Spectrometry Research Award (2012), the Molecular Cellular Proteomics Lectureship (2013), and the Mallinckrodt Scholar Award (2015).

Proteomics Tracing the Footsteps of Viral Infections


Every year, a major cause of human disease and death worldwide is infection with the various viral pathogens that are intrinsic to our ecosystem. The outcomes of infections derive from the dynamic interactions between viruses and host cells that function to promote either virus replication or host defense against invading pathogens. Thus, viral infection triggers an impressive range of proteome changes. Alterations in protein abundances, interactions, posttranslational modifications, subcellular localizations, and secretion are temporally regulated during the progression of an infection. Consequently, recent years have highlighted mass spectrometry-based proteomics as a core component of fundamental discoveries in virology. This presentation will discuss proteomic methods developed for studying virus-host protein interactions, as well as alterations in proteome composition and organization in space and time during the progression of infection. We have applied such methods to addressing three main questions: 1) what host cell conditions allow infections to be permissive, 2) how the host immune system responds to the infection, and 3) what are the mechanisms of pathogen replication and transmission? Examples will be given from our studies of innate immune response upon infection with herpesviruses, as well as of mechanisms through which viruses remodel subcellular organelle function to suppress host defense and promote viral replication. Such studies demonstrate how integrative omic technologies can help paint a picture of the pathogen’s life cycle and aid in the future development of antiviral therapies.