Robert Husson is interested in understanding the molecular pathogenesis of Mycobacterium tuberculosis infection, particularly the means by which the bacterium adapts to its host. Understanding the means by which the bacterium adapts to the host can identify novel anti-bacterial targets for the design of new therapeutics. The Husson laboratory has focused on two aspects of microbial adaptation:
- A major area of research in the Husson laboratory is the regulation of transcription by M. tuberculosis. We have characterized several sigma factors of M. tuberculosis, including SigE and SigH that are important in the response to oxidative and other stresses. Ongoing work indicates that these regulators are important in the response to starvation, oxidative and nitrosative stresses, and other challenges that are likely to be encountered during infection.
- The second major area of Dr. Husson's research focuses on signal transduction pathways of M. tuberculosis. In addition to the typical bacterial two-component signal transduction systems, the bacterium has genes encoding 11 eukaryotic-like serine/ threonine kinases. We are investigating two of these kinases, which are essential and appear to regulate cell division. We are working to identify the in vivo targets of these kinases, the signals that activate them, and to determine the function of these molecules in M. tuberculosis physiology. Using chemical biology and genetic approaches we are investigation the broad effects of these kinases on M. tuberculosis physiology.
In addition to this research on molecular pathogenesis, the Husson laboratory is undertaking translational research relevant to new approaches for the diagnosis and treatment of tuberculosis in children and adults.
About Robert Husson
Robert Husson received his MD from Harvard Medical School. He completed an internship, residency, and fellowship at Boston Children's Hospital. He undertook additional research training at Whitehead Institute and the National Institutes of Health prior to returning Boston Children’s Hospital.
- Kang C-M, Abbott DW, Park ST, Dascher CC, Cantley LC, Husson RN. The Mycobacterium tuberculosis serine/threonine kinases PknA and PknB: substrate identification and regulation of cell shape. Genes Dev 2005; 19: 1692-1704.
- Park ST, Kang C-M, Husson RN. Regulation of the SigH stress response regulon by an essential protein kinase in Mycobacterium tuberculosis. Proc Natl Acad Sci USA 2008; 105:13105-13110.
- Prisic A, Dankwa S, Schwartz D, Chou MF, Locasale J, Kang C-M, Bemis G, Church GM, Steen S, Husson RN. Extensive phosphorylation with overlapping specificity by Mycobacterium tuberculosis serine/threonine protein kinases Proc Natl Acad Sci USA 2010: 107:7521-7526. PMID: 20368441
- Mir M, Asong J, Li X, Cardot J, Boons G-J, Husson RN. The Extracellular domain of the Mycobacterium tuberculosis Ser/Thr Kinase PknB binds specific muropeptides and is required for PknB Localization. PLoS Pathogens 2011; 7:e1002182. PMID: 21829358.
- Sharp JD, Cruz JW, Raman S, Inouye M, Husson RN, Woychik NA. Growth and translation inhibition through sequence specific RNA binding by a Mycobacterium tuberculosis VAPC toxin. J Biol Chem 2012; 287(16): 12835–12847. doi:10.1074/jbc.M112.340109. PMID: 22354968
- Schifano JM, Edifor R, Ouyang M, Sharp JD, Konkimalla A, Husson RN, Woychik NA. Mycobacterial toxin MazF-mt6 inhibits translation through cleavage of 23S rRNA at the ribosomal A site. Proc Natl Acad Sci USA 2013;110:8501-8506. PMID:23650345.