Molecular interfaces of the galactose-binding protein Tectonin domains in host-pathogen interaction.

The Journal of Biological Chemistry
Diana Hooi Ping LowJeak Ling Ding

Abstract

Beta-propeller proteins function in catalysis, protein-protein interaction, cell cycle regulation, and innate immunity. The galactose-binding protein (GBP) from the plasma of the horseshoe crab, Carcinoscorpius rotundicauda, is a beta-propeller protein that functions in antimicrobial defense. Studies have shown that upon binding to Gram-negative bacterial lipopolysaccharide (LPS), GBP interacts with C-reactive protein (CRP) to form a pathogen-recognition complex, which helps to eliminate invading microbes. However, the molecular basis of interactions between GBP and LPS and how it interplays with CRP remain largely unknown. By homology modeling, we showed that GBP contains six beta-propeller/Tectonin domains. Ligand docking indicated that Tectonin domains 6 to 1 likely contain the LPS binding sites. Protein-protein interaction studies demonstrated that Tectonin domain 4 interacts most strongly with CRP. Hydrogen-deuterium exchange mass spectrometry mapped distinct sites of GBP that interact with LPS and with CRP, consistent with in silico predictions. Furthermore, infection condition (lowered Ca(2+) level) increases GBP-CRP affinity by 1000-fold. Resupplementing the system with a physiological level of Ca(2+) did not reverse th...Continue Reading

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Citations

Jun 26, 2014·Proceedings of the National Academy of Sciences of the United States of America·Richard D Cummings
Jun 1, 2014·Proceedings of the National Academy of Sciences of the United States of America·Therese WohlschlagerMarkus Künzler
May 18, 2011·Cell Host & Microbe·Michinaga OgawaChihiro Sasakawa
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Nov 3, 2010·The Journal of Immunology : Official Journal of the American Association of Immunologists·Jing ZhangJeak Ling Ding
Mar 14, 2019·Frontiers in Immunology·Donald N Ngwa, Alok Agrawal

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