Synthetic Polymer Affinity Ligand for Bacillus thuringiensis ( Bt) Cry1Ab/Ac Protein: The Use of Biomimicry Based on the Bt Protein-Insect Receptor Binding Mechanism

Journal of the American Chemical Society
Mingming LiuKenneth J Shea

Abstract

We report a novel strategy for creating abiotic Bacillus thuringiensis ( Bt) protein affinity ligands by biomimicry of the recognition process that takes place between Bt Cry1Ab/Ac proteins and insect receptor cadherin-like Bt-R1 proteins. Guided by this strategy, a library of synthetic polymer nanoparticles (NPs) was prepared and screened for binding to three epitopes 280FRGSAQGIEGS290, 368RRPFNIGINNQQ379 and 436FRSGFSNSSVSIIR449 located in loop α8, loop 2 and loop 3 of domain II of Bt Cry1Ab/Ac proteins. A negatively charged and hydrophilic nanoparticle (NP12) was found to have high affinity to one of the epitopes, 368RRPFNIGINNQQ379. This same NP also had specific binding ability to both Bt Cry1Ab and Bt Cry1Ac, proteins that share the same epitope, but very low affinity to Bt Cry2A, Bt Cry1C and Bt Cry1F closely related proteins that lack epitope homology. To locate possible NP- Bt Cry1Ab/Ac interaction sites, NP12 was used as a competitive inhibitor to block the binding of 865NITIHITDTNNK876, a specific recognition site in insect receptor Bt-R1, to 368RRPFNIGINNQQ379. The inhibition by NP12 reached as high as 84%, indicating that NP12 binds to Bt Cry1Ab/Ac proteins mainly via 368RRPFNIGINNQQ379. This epitope region was the...Continue Reading

References

Jun 6, 1998·Bioscience, Biotechnology, and Biochemistry·Y NagamatsuT Katsumoto
Sep 8, 1998·Microbiology and Molecular Biology Reviews : MMBR·E SchnepfD H Dean
Sep 8, 1998·Microbiology and Molecular Biology Reviews : MMBR·N CrickmoreD H Dean
Dec 11, 1999·Nature·D SaxenaG Stotzky
May 9, 2001·Biochimica Et Biophysica Acta·A Rachkov, N Minoura
Feb 24, 2004·Annual Review of Physiology·Janos K Lanyi
May 5, 2004·The Journal of Biological Chemistry·Gang HuaMichael J Adang
Jul 22, 2004·European Journal of Biochemistry·Juan L Jurat-Fuentes, Michael J Adang
Apr 7, 2005·Journal of Molecular Biology·Panadda BoonsermJade Li
Jul 8, 2005·Applied and Environmental Microbiology·Shogo AtsumiRyoichi Sato
Mar 10, 2006·Angewandte Chemie·Hidekazu NishinoKenneth J Shea
Jan 3, 2007·Toxicon : Official Journal of the International Society on Toxinology·Alejandra BravoMario Soberón
Jan 25, 2007·Insect Biochemistry and Molecular Biology·J A Fabrick, B E Tabashnik
Feb 3, 2007·Proceedings of the National Academy of Sciences of the United States of America·Tommy CedervallSara Linse
Jun 8, 2007·Microbiology and Molecular Biology Reviews : MMBR·Craig R Pigott, David J Ellar
Aug 4, 2007·Journal of the American Chemical Society·Mrinmoy DeVincent M Rotello
Oct 10, 2007·Proceedings of the National Academy of Sciences of the United States of America·E J Rosi-MarshallM L Stephen
Jan 30, 2008·Peptides·Luisa Elena FernándezMario Soberón
Oct 22, 2008·Applied and Environmental Microbiology·Carmen Sara Hernández-RodríguezJuan Ferré
Feb 24, 2010·The Journal of Biological Chemistry·Iván ArenasIsabel Gómez
Mar 11, 2011·Proceedings of the National Academy of Sciences of the United States of America·Daniel G IsomBertrand García-Moreno
Jun 15, 2011·ACS Applied Materials & Interfaces·Ying WangDavid G Whitten
Nov 8, 2011·Macromolecules·Michael H Smith, L Andrew Lyon
Dec 14, 2011·Chemical Society Reviews·Jayant KhandareRainer Haag
Dec 21, 2011·Accounts of Chemical Research·Michael H Smith, L Andrew Lyon
Dec 27, 2011·Proceedings of the National Academy of Sciences of the United States of America·Yu HoshinoKenneth J Shea
Jan 11, 2012·Journal of the American Chemical Society·Zhiyang ZengKenneth J Shea
Mar 1, 2012·Chemical Reviews·Tina VermondenWim E Hennink
Apr 3, 2012·Microbial Biotechnology·Alejandra BravoMario Soberón
Jul 31, 2012·Biochimica Et Biophysica Acta·I S MoreiraM J Ramos
Aug 29, 2012·Journal of the American Chemical Society·Shih-Hui LeeKenneth J Shea

❮ Previous
Next ❯

Related Concepts

Related Feeds

Adhesion Molecules in Health and Disease

Cell adhesion molecules are a subset of cell adhesion proteins located on the cell surface involved in binding with other cells or with the extracellular matrix in the process called cell adhesion. In essence, cell adhesion molecules help cells stick to each other and to their surroundings. Cell adhesion is a crucial component in maintaining tissue structure and function. Discover the latest research on adhesion molecule and their role in health and disease here.

Adherens Junctions

An adherens junction is defined as a cell junction whose cytoplasmic face is linked to the actin cytoskeleton. They can appear as bands encircling the cell (zonula adherens) or as spots of attachment to the extracellular matrix (adhesion plaques). Adherens junctions uniquely disassemble in uterine epithelial cells to allow the blastocyst to penetrate between epithelial cells. Discover the latest research on adherens junctions here.

Cadherins and Catenins

Cadherins (named for "calcium-dependent adhesion") are a type of cell adhesion molecule (CAM) that is important in the formation of adherens junctions to bind cells with each other. Catenins are a family of proteins found in complexes with cadherin cell adhesion molecules of animal cells: alpha-catenin can bind to β-catenin and can also bind actin. β-catenin binds the cytoplasmic domain of some cadherins. Discover the latest research on cadherins and catenins here.