2omy
From Proteopedia
Crystal structure of InlA S192N/hEC1 complex
Overview
In causing disease, pathogens outmaneuver host defenses through a dedicated arsenal of virulence determinants that specifically bind or modify individual host molecules. This dedication limits the intruder to a defined range of hosts. Newly emerging diseases mostly involve existing pathogens whose arsenal has been altered to allow them to infect previously inaccessible hosts. We have emulated this chance occurrence by extending the host range accessible to the human pathogen Listeria monocytogenes by the intestinal route to include the mouse. Analyzing the recognition complex of the listerial invasion protein InlA and its human receptor E-cadherin, we postulated and verified amino acid substitutions in InlA to increase its affinity for E-cadherin. Two single substitutions increase binding affinity by four orders of magnitude and extend binding specificity to include formerly incompatible murine E-cadherin. By rationally adapting a single protein, we thus create a versatile murine model of human listeriosis.
About this Structure
2OMY is a Protein complex structure of sequences from Homo sapiens and Listeria monocytogenes. Full crystallographic information is available from OCA.
Reference
Extending the host range of Listeria monocytogenes by rational protein design., Wollert T, Pasche B, Rochon M, Deppenmeier S, van den Heuvel J, Gruber AD, Heinz DW, Lengeling A, Schubert WD, Cell. 2007 Jun 1;129(5):891-902. PMID:17540170 Page seeded by OCA on Thu May 22 22:27:00 2008
