Project Details
Domain structure of proteobacterial adhesins and of related surface proteins
Applicant
Professor Dr. Andrei N. Lupas
Subject Area
Metabolism, Biochemistry and Genetics of Microorganisms
Term
from 2004 to 2008
Project identifier
Deutsche Forschungsgemeinschaft (DFG) - Project number 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 Programme
Research Units