Solution Structure of Spheniscin, a β-Defensin from the Penguin Stomach

Landon, C.; Thouzeau, Cécile; Labbé, H. J.; Bulet, Philippe; Vovelle, F.

doi:10.1074/jbc.m401338200

Cited by 43 publications

(42 citation statements)

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“…The determination of the first tridi-mensional NMR structures of king penguin AvBD103b and chicken AvBD2 defensins showed the disulfide bridge motif typical of ␤-defensins (i.e. C1-C5/C2-C4/C3-C6) (16,17), thus corroborating this terminology. Last, AvBDs generally possess antimicrobial activities against various microorganisms, including Gram-positive and Gram-negative bacteria as well as fungi (18 -21).…”

supporting

confidence: 59%

Three-dimensional NMR Structure of Hen Egg Gallin (Chicken Ovodefensin) Reveals a New Variation of the β-Defensin Fold

Hervé

Meudal

Labas

et al. 2014

Journal of Biological Chemistry

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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.

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confidence: 59%

Three-dimensional NMR Structure of Hen Egg Gallin (Chicken Ovodefensin) Reveals a New Variation of the β-Defensin Fold

Hervé

Meudal

Labas

et al. 2014

Journal of Biological Chemistry

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“…At 1 M NaCl, M. lysodeikticus did not grow in the control, and a low bacterial growth can be observed for the marine bacteria B. stationis. In contrast to most AMPs, Cg-Def seems to conserve its antibacterial activity at such a high salt concentration (30,31).…”

Section: Resultsmentioning

confidence: 99%

Characterization of a Defensin from the Oyster Crassostrea gigas

Gueguen

Herpin

Aumelas

et al. 2006

Journal of Biological Chemistry

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In invertebrates, defensins were found in arthropods and in the mussels. Here, we report for the first time the identification and characterization of a defensin (Cg-Def) from an oyster. Cg-def mRNA was isolated from Crassostrea gigas mantle using an expressed sequence tag approach. To gain insight into potential roles of Cg-Def in oyster immunity, we produced the recombinant peptide in Escherichia coli, characterized its antimicrobial activities, determined its solution structure by NMR spectroscopy, and quantified its gene expression in vivo following bacterial challenge of oysters. Recombinant Cg-Def was active in vitro against Grampositive bacteria but showed no or limited activities against Gramnegative bacteria and fungi. The activity of Cg-Def was retained in vitro at a salt concentration similar to that of seawater. The Cg-Def structure shares the so-called cystine-stabilized ␣-␤ motif (CS-␣␤) with arthropod defensins but is characterized by the presence of an additional disulfide bond, as previously observed in the mussel defensin (MGD-1). Nevertheless, despite a similar global fold, the Cg-Def and MGD-1 structures mainly differ by the size of their loops and by the presence of two aspartic residues in Cg-Def. Distribution of Cg-def mRNA in various oyster tissues revealed that Cgdef is mainly expressed in mantle edge where it was detected by mass spectrometry analyses. Furthermore, we observed that the Cg-def messenger concentration was unchanged after bacterial challenge. Our results suggest that Cg-def gene is continuously expressed in the mantle and would play a key role in oyster by providing a first line of defense against pathogen colonization. Antimicrobial peptides (AMPs)5 are important components of the innate immune system that have been conserved during evolution (1). They constitute a first line of host defense against pathogens in plants and animals (2, 3). We estimate that more than 1000 antimicrobial peptides have been described at the level of their primary structure (2). They are gathered in the Antimicrobial Sequence Database (www.bbcm.units.it/ϳtossi/amsdb.html). AMPs can be classified into three major groups: (i) linear peptides that form amphipathic ␣-helices, (ii) cyclic peptides containing cysteine-residue engaged in disulfide bonds, and (iii) peptides with an overrepresentation in certain amino acids (proline, arginine, glycine, or histidine). Despite their great diversity in terms of size, primary structure, amino acid composition, and mode of action, most AMPs are characterized by the preponderance in cationic and hydrophobic amino acids (2). In most of the cases, this amphipathic character is considered as crucial for the interaction of the effective peptide with the membrane of sensitive microorganisms. This first interaction seems to be essential whatever the exact mode of action: (i) through disruption of their negatively charged cytoplasmic membranes or (ii) through killing following translocation into the bacteria without membrane lyses and binding to a specific target pr...

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“…P81534), which seems to include the biologically active part of the molecule (14). Solving the three-dimensional structure by two-dimensional nuclear magnetic resonance and molecular modeling is needed in order to determine the pairing pattern of the six disulfide bridges and to understand the structure-function relationship of AvBD11, as has been performed for AvBD103b (15). Avian ␤-defensins interact electrostatically with negatively charged components of bacterial membranes, such as lipopolysaccharides, lipoteichoic acid, and anionic phospholipids.…”

Section: Discussionmentioning

confidence: 99%

“…AvBD103b was isolated from the stomach contents of the king penguin and exhibits a wide spectrum of antimicrobial activity against Gram-positive and Gram-negative bacteria, yeasts, and fungi (29). The high potency of AvBD103b against bacteria was correlated with its extreme cationicity but also with the presence of a hydrophobic patch which is not present in mammalian ␤-defensins (15).…”

mentioning

confidence: 99%

“…Only the three-dimensional structure of the king penguin avian ␤-defensin 103b, (AvBD103b or spheniscin-2) has been solved recently. The tertiary structure of AvBD103b is very similar to those of mammalian ␤-defensins, including the common array of disulfide bonds and the presence of a three-stranded ␤-sheet as the main secondary structure element (15,26). AvBD103b was isolated from the stomach contents of the king penguin and exhibits a wide spectrum of antimicrobial activity against Gram-positive and Gram-negative bacteria, yeasts, and fungi (29).…”

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confidence: 99%

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Purification and Characterization of Avian β-Defensin 11, an Antimicrobial Peptide of the Hen Egg

Hervé-Grépinet

Réhault-Godbert

Labas

et al. 2010

Antimicrob Agents Chemother

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Natural antimicrobial peptides are present in different compartments (eggshell, egg white, and vitelline membranes) of the hen egg and are expected to be involved in the protection of the embryo during its development and to contribute to the production of pathogen-free eggs. In the present study, we used vitelline membranes from hen (Gallus gallus) eggs as a source of avian ␤-defensin 11 (AvBD11). A purification scheme using affinity chromatography and reverse-phase chromatography was developed. Purified AvBD11 was analyzed by a combination of mass spectrometry approaches to characterize its primary sequence and structure. A monoisotopic molecular species at [M ؉ H]؉ of 9,271.56 Da was obtained, and its N-and C-terminal sequences were determined. We also examined posttranslational modifications and identified the presence of 6 internal disulfide bonds. AvBD11 was found to exhibit antimicrobial activity toward both Gram-positive and Gram-negative bacteria.The avian egg is a unique and original biological system which is formed according to a well-defined spatial and temporal sequence as it passes along the reproductive tract of the hen. The segments of the oviduct involved in the egg formation are the infundibulum, the magnum, the isthmus, and the uterus. Each segment expresses and secretes specific molecules that become successively incorporated into the vitelline membranes in the infundibulum, the egg white in the magnum, the eggshell membranes in the isthmus, and the eggshell in the uterus. Thus, the hen deposits into the egg, which can be considered a closed chamber, all the nutrients and protective systems that are necessary to support the development of an embryo during 21 days of incubation. Recently, transcriptomic and proteomic approaches have identified almost 1,000 putative proteins and peptides in the various compartments of eggs (6). Among these are a number of polypeptides that are likely to resist microbial contamination of the eggs, some of which belong to the family of avian ␤-defensins (AvBDs).A total of 14 avian ␤-defensin genes have been identified through in silico studies. Because most of them were simultaneously described by two research groups, some confusion was generated due to different nomenclatures (9,10,18,31). In a collaborative venture, we proposed a novel nomenclature that adopted the numbering system used by Xiao et al. (31) and replaced the term "gallinacin," used formerly by Lehrer's group, with "avian ␤-defensin" (AvBD) (19). AvBDs are small cationic nonglycosylated peptides (1 to 9 kDa). Some of them were successfully tested for their antimicrobial activity, including chicken AvBDs AvBD1, -2, -7, and -9, turkey AvBD1 and -2, ostrich AvBDs AvBD1, -2, -7, and -8, and penguin AvBD103b (3, 30). In mammals, ␤-defensins are molecules of innate and adaptive immunity, with a broad spectrum of antimicrobial activity (1). ␤-Defensin molecules possess six highly conserved cysteines with the following consensus sequence motif, where C is a cysteine, G a glycine, and X any amino acid: X...

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Solution Structure of Spheniscin, a β-Defensin from the Penguin Stomach

Cited by 43 publications

References 42 publications

Three-dimensional NMR Structure of Hen Egg Gallin (Chicken Ovodefensin) Reveals a New Variation of the β-Defensin Fold

Three-dimensional NMR Structure of Hen Egg Gallin (Chicken Ovodefensin) Reveals a New Variation of the β-Defensin Fold

Characterization of a Defensin from the Oyster Crassostrea gigas

Purification and Characterization of Avian β-Defensin 11, an Antimicrobial Peptide of the Hen Egg

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