Graduate Studies Faculty
Eric D. Cambronne, Ph.D.
Programs:Molecular Microbiology & Immunology
Program in Molecular & Cellular Biosciences
Research Interests:Bacterial Pathogenesis, Type IV Secretion, Legionella pneumophila, Coxiella burnetii » Click here for more about Dr. Cambronne's research » PubMed Listing
Preceptor RotationsDr. Cambronne has not indicated availability for preceptor rotations at this time.
Faculty MentorshipDr. Cambronne has not indicated availability as a mentor at this time.
Numerous Gram-negative bacterial pathogens, including several CDC designated select agents have adopted a pathogenic strategy called type IV secretion. This process involves the direct inter-kingdom transport of virulence factors called ‘effector’ proteins from bacterium to host. Effector proteins function in the subversion of normal host cell processes to promote a favorable environment for bacterial replication. Importantly, type IV secretion represents a primary virulence determinant for the manifestation of several threatening human diseases. The focus of research in the Cambronne laboratory is the elucidation of molecular mechanisms involved in the recognition and transport of effector proteins by the type IV secretion pathway. We use the intracellular pathogen Legionella pneumophila, the causative agent of a severe pneumonia called Legionnaires’ disease as a model system for 1) Identification and characterization of specific secretion determinants on Legionella effector proteins, 2) Definition of the type IV secretion pathway, and 3) Surrogate host for defining secretion determinants on effector proteins from the obligate intracellular pathogen Coxiella burnetii. We hypothesize that type IV secretion determinants on effector proteins are largely conserved. Defining the physical attributes associated with type IV secretion signals will be applied to the identification of virulence factors from organisms that are genetically intractable. Further, assigning mechanisms required for type IV-mediated translocation will provide excellent targets for novel therapeutic development. We have identified a chaperone complex that is necessary for the transport of multiple effector proteins by L.pneumophila (PLoS Pathog. 2007 Dec;3(12):e188). The complex is necessary for the intracellular survival of L.pneumophila, and thus represents a critical stage in substrate recognition. Current work is exploring the potential for targeting this chaperone-effector interaction as a means for abrogating intracellular growth of L.pneumophila. Importantly, similar chaperone systems have emerged in other pathogens that utilize type IV secretion, making the implications of these studies highly significant to the combat of bacterial diseases.