Domain structure of proteobacterial adhesins and of related surface proteins

• Antragsteller: Professor Dr. Andrei N. Lupas
• Fachliche Zuordnung: Stoffwechselphysiologie, Biochemie und Genetik der Mikroorganismen
• Förderung: Förderung von 2004 bis 2008
• Projektkennung: Deutsche Forschungsgemeinschaft (DFG) - Projektnummer 5468788

Non-fimbrial adhesins are key virulence factors, required for the attachment of many pathogenic proteobacteria to host cells. They form an important group of surface proteins, whose sequence and structure are as yet poorly understood. We provided the first bioinformatic analysis of a non-fimbrial adhesin, YadA, which helped us define this family in terms of a conserved oligomeric membrane anchor domain with putative autotransporter function. We also discovered that domains of non-fimbrial adhesins were widely represented in the surface proteins of pathogenic and non-pathogenic proteobacteria, alike, suggesting an important role in the formation of surface structures. We are interested in using these observations as a starting point for providing a comprehensive description of the domain complement found in the surface proteins of proteobacteria. We propose to capture bioinformatic descriptors for each domain type into a public web system that allows the rapid annotation of newly determined sequences. We further propose to use the bioinformatic analyses to define the most important domain types, which we will clone, purify, and investigate by biomolecular NMR and other structural techniques.

• DFG-Verfahren: Forschungsgruppen
• Teilprojekt zu: FOR 449: Bakterielle Zellhülle: Synthese, Funktion und Wirkort