The NRW Research School BioStruct – Biological Structures in
Molecular Medicine and Biotechnology at Heinrich-Heine-University Duesseldorf in Germany, funded by the Ministry of Innovation, Science
and Research of the German Federal State North Rhine-Westphalia
(NRW), and the school chairmen Prof. Dr. Lutz Schmitt and Prof. Dr. Dieter Willbold invite applications on PhD Scholarships
starting in January 2012.
BioStruct offers innovative PhD education and research programs within a stimulating interdisciplinary environment combining the field of structural biology with molecular medicine and biotechnology. Highly motivated and excellent candidates holding an MSc or Diploma degree in the fields of Biochemistry, Biology, Chemistry, Physics and related fields can directly apply for a PhD Scholarship for the project "Structure and function of the Chlamydia adhesins OmcB and Pmp21” including a monthly stipend of 1345,- EUR and contributions towards travel and research expenses.
The ideal candidate will have a background in protein biochemistry and biophysical characterization of proteins. A strong interest in infection biology as well as in structural biology is a prerequisite.
Workplace will be the Heinrich Heine University Düsseldorf in the group of Prof. Dr. Johannes Hegemann.
Only complete applications according to the BioStruct application regulations will be considered. For further information please visit: www.biostruct.de
PhD Research Project Summary:
Chlamydiae are obligate intracellular bacterial pathogens which cause a variety of important human diseases. Chlamydia trachomatis is the most common bacterial agent of sexually transmitted diseases and is responsible for over 90 million new infections every year worldwide. The C. trachomatis ocular serovars are responsible for trachoma, the major cause of preventable blindness in developing countries. Acute C. pneumoniae infections cause pulmonary diseases (e.g. 10 % of all pneumonia incidents worldwide), whereas the chronic infection is linked to atherosclerosis and artery disease. The chlamydial infection starts with the adhesion of the bacteria to the human cell by binding of bacterial adhesins to eukaryotic receptors.
We have identified and characterised the first chlamydial adhesin proteins which interact with the human cell. The OmcB protein binds to heparan sulfate-like glycosaminoglycan (GAG) structures on the human cell surface. Single amino acids in the GAG-binding domain of OmcB are essential for adhesion to human cells and may determine cell tropism and disease pattern for different C. trachomatis serovars (systemic versus local infection). The second adhesin recently identified consists of a family of 21 related polymorphic membrane proteins (Pmp) unique to Chlamydiae, whose human cell surface receptor has just been identified. Pmp proteins are anchored in the bacterial membrane and their N-termini carry several independent adhesion domains.
Analysis of the three-dimensional structure of the adhesins OmcB and Pmp21 (as prototype) will form the basis for a molecular understanding of the interactions of these proteins with their human receptors and will facilitate identification of small molecule inhibitors.
For further information on the NRW Research School BioStruct, prerequisites and mandatory application forms please visit our website: www.biostruct.de
Application Deadline for the current call: December 20th, 2011
BioStruct offers innovative PhD education and research programs within a stimulating interdisciplinary environment combining the field of structural biology with molecular medicine and biotechnology. Highly motivated and excellent candidates holding an MSc or Diploma degree in the fields of Biochemistry, Biology, Chemistry, Physics and related fields can directly apply for a PhD Scholarship for the project "Structure and function of the Chlamydia adhesins OmcB and Pmp21” including a monthly stipend of 1345,- EUR and contributions towards travel and research expenses.
The ideal candidate will have a background in protein biochemistry and biophysical characterization of proteins. A strong interest in infection biology as well as in structural biology is a prerequisite.
Workplace will be the Heinrich Heine University Düsseldorf in the group of Prof. Dr. Johannes Hegemann.
Only complete applications according to the BioStruct application regulations will be considered. For further information please visit: www.biostruct.de
PhD Research Project Summary:
Chlamydiae are obligate intracellular bacterial pathogens which cause a variety of important human diseases. Chlamydia trachomatis is the most common bacterial agent of sexually transmitted diseases and is responsible for over 90 million new infections every year worldwide. The C. trachomatis ocular serovars are responsible for trachoma, the major cause of preventable blindness in developing countries. Acute C. pneumoniae infections cause pulmonary diseases (e.g. 10 % of all pneumonia incidents worldwide), whereas the chronic infection is linked to atherosclerosis and artery disease. The chlamydial infection starts with the adhesion of the bacteria to the human cell by binding of bacterial adhesins to eukaryotic receptors.
We have identified and characterised the first chlamydial adhesin proteins which interact with the human cell. The OmcB protein binds to heparan sulfate-like glycosaminoglycan (GAG) structures on the human cell surface. Single amino acids in the GAG-binding domain of OmcB are essential for adhesion to human cells and may determine cell tropism and disease pattern for different C. trachomatis serovars (systemic versus local infection). The second adhesin recently identified consists of a family of 21 related polymorphic membrane proteins (Pmp) unique to Chlamydiae, whose human cell surface receptor has just been identified. Pmp proteins are anchored in the bacterial membrane and their N-termini carry several independent adhesion domains.
Analysis of the three-dimensional structure of the adhesins OmcB and Pmp21 (as prototype) will form the basis for a molecular understanding of the interactions of these proteins with their human receptors and will facilitate identification of small molecule inhibitors.
For further information on the NRW Research School BioStruct, prerequisites and mandatory application forms please visit our website: www.biostruct.de
Application Deadline for the current call: December 20th, 2011
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