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Cloning of cDNA sequences encoding cowpea (Vigna unguiculata) vicilins: Computational simulations suggest a binding mode of cowpea vicilins to chitin oligomers.
- Source :
-
International journal of biological macromolecules [Int J Biol Macromol] 2018 Oct 01; Vol. 117, pp. 565-573. Date of Electronic Publication: 2018 May 27. - Publication Year :
- 2018
-
Abstract
- Vicilins are 7S globulins which constitute the major seed storage proteins in leguminous species. Variant vicilins showing differential binding affinities for chitin have been implicated in the resistance and susceptibility of cowpea to the bruchid Callosobruchus maculatus. These proteins are members of the cupin superfamily, which includes a wide variety of enzymes and non-catalytic seed storage proteins. The cupin fold does not share similarity with any known chitin-biding domain. Therefore, it is poorly understood how these storage proteins bind to chitin. In this work, partial cDNA sequences encoding β-vignin, the major component of cowpea vicilins, were obtained from developing seeds. Three-dimensional molecular models of β-vignin showed the characteristic cupin fold and computational simulations revealed that each vicilin trimer contained 3 chitin-binding sites. Interaction models showed that chito-oligosaccharides bound to β-vignin were stabilized mainly by hydrogen bonds, a common structural feature of typical carbohydrate-binding proteins. Furthermore, many of the residues involved in the chitin-binding sites of β-vignin are conserved in other 7S globulins. These results support previous experimental evidences on the ability of vicilin-like proteins from cowpea and other leguminous species to bind in vitro to chitin as well as in vivo to chitinous structures of larval C. maculatus midgut.<br /> (Copyright © 2018 Elsevier B.V. All rights reserved.)
- Subjects :
- Animals
Binding Sites
Chitin chemistry
Chitin genetics
Cloning, Molecular
Coleoptera pathogenicity
DNA, Complementary genetics
Disease Resistance genetics
Plant Diseases genetics
Plant Diseases parasitology
Plant Proteins chemistry
Protein Binding
Seed Storage Proteins chemistry
Seeds chemistry
Seeds genetics
Vigna growth & development
Plant Proteins genetics
Seed Storage Proteins genetics
Vigna genetics
Subjects
Details
- Language :
- English
- ISSN :
- 1879-0003
- Volume :
- 117
- Database :
- MEDLINE
- Journal :
- International journal of biological macromolecules
- Publication Type :
- Academic Journal
- Accession number :
- 29847781
- Full Text :
- https://doi.org/10.1016/j.ijbiomac.2018.05.197