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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Nys, Yves Réhault-godbert, Sophie Landon, Céline Meudal, Hervé Gautron, Joël Hervé, Virginie Labas, Valérie Berges, Magali Guyot, Nicolas Delmas, Agnès F. |
| Description | Author Affiliation: Hervé V ( From Institut National de la Recherche Agronomique (INRA), UR83 Recherches Avicoles, Fonction et Régulation des Protéines de l'Å uf, F-37380 Nouzilly, France.) |
| Abstract | Gallin is a 41-residue protein, first identified as a minor component of hen egg white and found to be antimicrobial against Escherichia coli. Gallin may participate in the protection of the embryo during its development in the egg. Its sequence is related to antimicrobial ß-defensin peptides. In the present study, gallin was chemically synthesized 1) to further investigate its antimicrobial spectrum and 2) to solve its three-dimensional NMR structure and thus gain insight into structure-function relationships, a prerequisite to understanding its mode(s) of action. Antibacterial assays confirmed that gallin was active against Escherichia coli, but no additional antibacterial activity was observed against the other Gram-positive or Gram-negative bacteria tested. The three-dimensional structure of gallin, which is the first ovodefensin structure to have been solved to date, displays a new five-stranded arrangement. The gallin three-dimensional fold contains the three-stranded antiparallel ß-sheet and the disulfide bridge array typical of vertebrate ß-defensins. Gallin can therefore be unambiguously classified as a ß-defensin. However, an additional short two-stranded ß-sheet reveals that gallin and presumably the other ovodefensins form a new structural subfamily of ß-defensins. Moreover, gallin and the other ovodefensins calculated by homology modeling exhibit atypical hydrophobic surface properties, compared with the already known vertebrate ß-defensins. These specific structural features of gallin might be related to its restricted activity against E. coli and/or to other yet unknown functions. This work provides initial understanding of a critical sequence-structure-function relationship for the ovodefensin family. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 10 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-03-07 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Metabolism Beta-Defensins Chemistry Amino Acid Sequence Animals Imaging, Three-Dimensional Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular Protein Folding Chemical Synthesis Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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