Dr. Ken Dimock
Please note: Dr. Dimock is no longer accepting any graduate students
Professor
Degree:
B.Sc. (N.B.), Ph.D. (Van.)Contact info:
Roger Guindon Hall, Rm. 4163
Phone:
613-562-5800 x 8958
613-562-5800 x 8311 (lab)
Email: kdimock@uottawa.ca
Research Interests:
For a virus to infect a cell, it must first bind to a receptor on the cell surface (attachment) and then deliver its genetic material into the interior of the cell (penetration), where it can initiate viral transcription, protein synthesis and replication. Virus binding to a receptor is only the first of several interactions between a virus and host cell surface molecules that are necessary for infection to occur. In our lab we are using molecular methods in an effort to understand these early stages of virus infection. Specifically, we analyze interactions within viral proteins, between viral proteins, and between viral proteins and host proteins, that are important for virus attachment and entry.
For example, we have shown that decay-accelerating factor (DAF) is a binding protein for one of the viruses that we study, enterovirus 70 (EV70), a causative agent of an epidemic form of conjunctivitis. We are examining the nature of the interaction between DAF and EV70. The expression of DAF on the surface of a cell, however, does not ensure infection and other cellular proteins (coreceptors) must be involved EV70 entry. We are attempting to identify these coreceptors and, ultimately, how they interact with EV70 polypeptides.
We also work with human parainfluenza virus 3 (HPIV3), which is an important agent of respiratory infections. In infants, HPIV3 infection can lead to bronchiolitis or pneumonia. HPIV3 virions contain 2 surface glycoproteins: HN, the receptor- binding protein, and F, which is directly responsible for the delivery of the HPIV3 genome into cells via fusion of the viral membrane with the plasma membrane of the host cell. To better understand the relationship between F protein structure and its function, we are mapping regions in the F protein that are involved either in intramolecular interactions that correctly fold the molecule, or for complex formation with HN, which is essential for fusion activity.
By learning more about the molecular nature of protein-protein interactions involved in viral entry processes, we hope to identify potential targets for antiviral therapy.