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Conference Announcement
"Immunodiagnosis of tuberculosis: new questions, new tools" |
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The Public Health Research Institute of the New Jersey Medical School and the Statens Serum Institut,
Copenhagen, Denmark, under the auspices of the STOP TB Working Group on Diagnostics,
and with the support of the Foundation for New and Innovative Diagnostics (FIND), the Special
Program for Research and Training in Tropical Diseases (TDR) at the World Health Organization,
the US National Institute of Allergy and Infectious Diseases, are organizing an International
Conference on "Immunodiagnosis of tuberculosis: new questions, new tools"
The goal of the conference is to stimulate interdisciplinary discussion and promote collaboration
among scientists having different but related interests. These range from basic microbiology and
immunology, to the science of establishing field studies, and to research leading to new strategies
of biomarker discovery and new assay platforms. A challenging area such as the immunodiagnosis
of TB in children will be discussed in a dedicated session.
Location
The conference will be held from September 21 – 23, 2008, at the Founder's Inn & Spa,
Virginia Beach,VA, USA.
Program
The program includes a keynote talk (evening of day 1), six plenary sessions and two poster sessions
(days 2 and 3). Speakers will also be selected from among those submitting abstracts for poster presentation.
The anticipated number of participants is 200. The conference proceedings will be published in a specialized
journal.
Travel Awards
A limited number of junior travel awards will be available for junior investigators from developing countries.
Invited speakers
- Sandra Arend, Leiden University Medical Center, Leiden, the Netherlands
- Joe Bellanti, Georgetown University Medical Center, Washington, DC, USA
- Mark Doherty, Statens Serum Institut, Copenhagen, Denmark
- Steven Elledge, Harvard University, Cambridge, MA, USA
- * Philip Felgner, University of California, Irvine, CA, USA
- Sebastien Gagneux, MRC National Institute for Medical Research, London, United Kingdom
- Marila Gennaro, Public Health Research Institute, University of Medicine and Dentistry, Newark, NJ, USA
- * Anneke Hesseling, Stellenbosch University, Cape Town, South Africa
- Elaine Holmes, Imperial College, London, United Kingdom
- * Stefan Kaufmann, Max Planck Institute for Infection Biology, Berlin, Germany
- Abraham Lee, University of California, Irvine, CA, USA
- JohnJoe McFadden, University of Surrey, United Kingdom
- * Dick Menzies, McGill University, Montreal, Quebec, Canada
- Adrian Ozinsky, Institute for Systems Biology, Seattle, WA, USA
- Mark Perkins, Foundation for New and Innovative Diagnostics, Geneva, Switzerland
- Mario Raviglione, Stop TB Department, World Health Organization, Geneva, Switzerland (Keynote Lecture)
- * Mario Roederer, National Institute of Allergy and Infectious Diseases, Bethesda, MD, USA
- Padmini Salgame, University of Medicine and Dentistry, Newark, NJ, USA
- Markus Wenk, National University of Singapore, Singapore
- * Douglas Young, Imperial College, London, United Kingdom
*) chairs
Organizers: Dr. Marila Gennaro from the Public Health Research Institute and
Dr. Mark Doherty from the Statens Serum Institut, Copenhagen, Denmark
For more information and registration, please visit the conference's website at www.tb-conference.com
To download the conference announcement, please follow this link .
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Paper Highlight |
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The PhoP-PhoR two-component system is essential for the virulence of Mycobacterium tuberculosis.
Global gene expression profiling indicates that the response regulator, PhoP, regulates expression of over 110 genes in M. tuberculosis.
To study the regulatory mechanism of PhoP, Shuishu Wang, Jean Engohang-Ndong, and Issar Smith (Biochemistry, 2007, published on Web 12/01/2007, bi700970a) determined the crystal structure of the C-terminal DNA-binding domain of PhoP (PhoPC).
The PhoPC structure consists of a three-helical bundle sandwiched between the N-terminal ß-sheet and the C-terminal ß-sheet.
The structure and electrostatic potential surface of PhoPC closely resemble those of the DNA-binding domain of PhoB from E. coli, suggesting that they bind DNA in a similar way.
Structural comparison reveals residues that are likely to play important roles in DNA binding and nucleotide sequence recognition.
The authors are now working on the structure of the full-length PhoP and are also in the process of determining the structure of PhoR, the cognitive histidine kinase.
The structural information will be helpful in developing PhoP and PhoR as targets for new anti-tuberculosis therapies.
Download publication
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