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Membrane-SPINE: A Biochemical Tool to Identify Protein-protein Interactions of Membrane Proteins In Vivo
Published on: November 7, 2013
Membrane activity of a C-reactive protein
John M Harrington1, Hui-Ting Chou, Thomas Gutsmann
1Department of Molecular and Cellular Biology, University of California, Davis, CA 95616, USA. jmharrin@uga.edu
FEBS Letters
|February 24, 2009
Summary
Limulus C-reactive protein (L-CRP) forms fibers that trap liposomes and bind to bacteria. This interaction alters bacterial membrane properties, suggesting L-CRP
Area of Science:
- Biochemistry
- Immunology
- Microbiology
Background:
- C-reactive protein (CRP) from the horseshoe crab Limulus polyphemus displays intricate membrane interactions.
- Understanding these interactions is crucial for elucidating innate immune responses against pathogens.
Purpose of the Study:
- To investigate the behavior of Limulus C-reactive protein (L-CRP) and lipids during interactions with model liposomes and bacterial membranes.
- To characterize the effects of L-CRP on the mechano-elastic properties of bacterial membranes.
Main Methods:
- Utilized model liposomes and Gram-negative bacteria for in vitro interaction studies with L-CRP.
- Employed techniques to observe L-CRP's structural changes (fibril formation) and binding to bacterial surfaces.
- Measured and compared the mechano-elastic properties of L-CRP-treated and untreated bacterial membranes.
Main Results:
- L-CRP forms extended fibrillar structures that encapsulate liposomes in the presence of Ca(2+).
- Observed L-CRP fibers bound to the surface of Gram-negative bacteria.
- L-CRP treatment significantly altered the mechano-elastic properties of bacterial membranes, inducing rigidification and domain reorganization.
Conclusions:
- L-CRP exhibits complex membrane activities, including fibril formation and bacterial surface binding.
- These interactions lead to significant changes in bacterial membrane properties.
- Suggests a role for L-CRP as a defense molecule involved in pathogen entrapment and elimination.
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