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SYNKNØYT-Progr.f.synkrotron- og nøytron

Microbial recognition investigated by membrane protein crystallography

Awarded: NOK 3.6 mill.

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2009 - 2013


The main goal of this project is to structurally and functionally characterize the molecular interactions underlying infection by the common gastric pathogen H. pylori. This will not only lead to a better understanding of the fundamental molecular recogni tion mechanisms, but also put us in a position to develop new tools for disease intervention. This project is part of a broader investigation by us, directed at the role of blood group antigens in pathogenesis, as the blood group of individuals has been s hown to correlate with the severity of disease in a number of bacterial infections. Understanding the underlying molecular recognition processes may eventually provide us with important leads towards patient-specific treatment and prevention strategies. This project is very challenging, as it deals with the structure determination of membrane proteins. Membrane protein structure determination has two major bottlenecks: the production of the protein sample in sufficient amounts and protein crystallization . In this case, protein production is a minor issue, at least for BabA, as 30% of the total protein content of H. pylori consists of BabA, its major blood group antigen binding adhesin. However, membrane protein crystallization is notoriously difficult an d membrane protein crystals are often of inferior quality, making extensive synchrotron use a necessity. This project will pave the way to the establishment of membrane protein crystallography in Norway.


SYNKNØYT-Progr.f.synkrotron- og nøytron