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Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Published on: July 5, 2018
Crystal structure of a chimeric receptor binding protein constructed from two lactococcal phages
Marina Siponen1, Silvia Spinelli, Stéphanie Blangy
1Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS, and Universités Aix-Marseille I & II, Campus de Luminy, Case 932, 13288 Marseille Cedex 09, France.
Journal of Bacteriology
|March 17, 2009
Summary
Researchers created a hybrid phage receptor binding protein (RBP) by combining domains from different Lactococcus lactis phages. The resulting chimera maintained structural integrity and effectively bound glycerol, offering insights into phage-host interactions.
Area of Science:
- Bacteriophage biology
- Structural biology
- Dairy microbiology
Background:
- Lactococcus lactis, crucial for dairy production, is susceptible to phage infections.
- Receptor Binding Proteins (RBPs) on phages mediate host recognition and infection.
- Previous studies characterized RBPs from phages TP901-1 (P335 group) and p2/bIL170 (936 group).
Purpose of the Study:
- To design and structurally characterize a novel RBP chimera.
- To investigate the structural stability and binding properties of the chimera.
- To understand domain interactions in phage RBPs.
Main Methods:
- Genetic engineering to create an RBP chimera (TP901-1 N-terminal/linker domains fused to p2 C-terminal domain).
- Protein expression and purification.
- X-ray crystallography to determine the chimera's three-dimensional structure.
- Binding affinity assays.
Main Results:
- The RBP chimera demonstrated structural stability, closely resembling parental structures.
- A minor linker displacement facilitated efficient RBP domain adaptation.
- The chimera's receptor binding site was structurally identical to the native p2 RBP.
- The chimera exhibited high-affinity binding to glycerol.
Conclusions:
- Hybrid phage RBPs can be structurally stable and functionally active.
- Domain swapping in RBPs offers a strategy to study host-phage interactions.
- The C-terminal domain dictates receptor binding specificity, even in a chimeric context.
