Three-dimensional NMR Structure of Hen Egg Gallin (Chicken Ovodefensin) Reveals a New Variation of the β-Defensin Fold
| Autor: | Joël Gautron, Sophie Réhault-Godbert, Agnès F. Delmas, Yves Nys, Nicolas Guyot, Virginie Hervé, Magali Berges, Céline Landon, Valérie Labas, Hervé Meudal |
|---|---|
| Přispěvatelé: | INRA (UR83 Recherches Avicoles F-37380 Nouzilly, France), Institut National de la Recherche Agronomique (INRA), Centre de biophysique moléculaire (CBM), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Plateforme d’Analyse Intégrative des Biomolécules et de Phénomique des Animaux d’Intérêt Bio-agronomique, Station de Recherches Avicoles (SRA), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Institut de Chimie du CNRS (INC), French National Research Agency (OVO-mining) [ANR-09-BLAN-0136], Unité de Recherches Avicoles (URA), Université d'Orléans (UO)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS), NOCCHI, ESTELLE |
| Rok vydání: | 2014 |
| Předmět: |
Protein Folding
animal structures beta-Defensins Molecular Sequence Data Antimicrobial peptides Biology peptide antimicrobien Antiparallel (biochemistry) medicine.disease_cause [SDV.IMM.II]Life Sciences [q-bio]/Immunology/Innate immunity [SDV.MHEP.PSR]Life Sciences [q-bio]/Human health and pathology/Pulmonology and respiratory tract Biochemistry Imaging Three-Dimensional Protein structure [SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseases medicine Animals Amino Acid Sequence Homology modeling Nuclear Magnetic Resonance Biomolecular [SDV.IMM.II] Life Sciences [q-bio]/Immunology/Innate immunity Molecular Biology Defensin Escherichia coli Peptide sequence ComputingMilieux_MISCELLANEOUS oeuf de poule integumentary system protection cellulaire fungi Cell Biology respiratory system bacterial infections and mycoses protéine de structure Protein Structure and Folding [SDV.MHEP.MI] Life Sciences [q-bio]/Human health and pathology/Infectious diseases [SDV.MHEP.PSR] Life Sciences [q-bio]/Human health and pathology/Pulmonology and respiratory tract réponse de l'hôte Protein folding escherichia coli Chickens défensine aviaire |
| Zdroj: | Journal of Biological Physics and Chemistry Journal of Biological Physics and Chemistry, Basel, Switzerland : Collegium Basilea (Institute of Advanced Study) ; Tbilisi : Association of Modern Scientific Investigation (AMSI), 2014, 289 (10), pp.7211-20. ⟨10.1074/jbc.M113.507046⟩ Journal of Biological Chemistry 10 (289), 7211-7220. (2014) Journal of Biological Physics and Chemistry, 2014, 289 (10), pp.7211-20. ⟨10.1074/jbc.M113.507046⟩ |
| ISSN: | 0021-9258 1512-0856 |
| DOI: | 10.1074/jbc.m113.507046 |
| Popis: | International audience; Background: Ovodefensins are small peptides from eggs, related to avian antimicrobial defensins. Results: The first three-dimensional structure of ovodefensins (gallin) is solved, and its antimicrobial properties are screened. Conclusion: Gallin adopts a -defensin fold, with significant variations. Its antibacterial spectrum was restricted to E. coli. Significance: The first structural features may be related to E. coli specificity and/or other yet unknown functions. 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 -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 -sheet and the disulfide bridge array typical of vertebrate -defensins. Gallin can therefore be unambiguously classified as a -defensin. However, an additional short two-stranded -sheet reveals that gallin and presumably the other ovodefensins form a new structural subfamily of -defensins. Moreover, gallin and the other ovodefensins calculated by homology modeling exhibit atypical hydrophobic surface properties, compared with the already known vertebrate -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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|