Dicynthaurin: an antimicrobial peptide from hemocytes of the solitary tunicate, Halocynthia aurantium

Lee, In Hee; Lee, Young S.; Kim, Chong Han; Kim, Chung Ryul; Hong, Teresa; Menzel, Lorenzo P.; Boo, Lee Ming; Pohl, Jan; Sherman, Mark A.; Waring, Alan J.; Lehrer, Robert I.

doi:10.1016/s0304-4165(01)00156-8

Cited by 86 publications

(68 citation statements)

References 35 publications

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“…In fact, even at 200 M, D1 could not significantly disrupt erythrocyte membranes (Ͻ5%). These results were very similar to those reported for dicynthaurin and halocidin (8,9), suggesting a common specificity of these peptides toward bacterial membranes.…”

Section: Resultssupporting

confidence: 89%

“…Recently, other hetero-and homodimeric peptides with bactericidal properties have been isolated in hemocytes of Halocynthia aurantium (8,9) and mouse intestinal tissues (10), namely dicynthaurin, halocidin, and cryptidin-related sequence peptides. Spectroscopic analysis has demonstrated that dicynthaurin and halocidin have a propensity to assume an ␣-helical conformation; the others are highly homologous to peptides with a relatively rigid antiparallel ␤-sheet structure.…”

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confidence: 99%

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A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin

Raimondo

Andreotti

Saint

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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Many bioactive peptides, presenting an unstructured conformation in aqueous solution, are made resistant to degradation by posttranslational modifications. Here, we describe how molecular oligomerization in aqueous solution can generate a still unknown transport form for amphipathic peptides, which is more compact and resistant to proteases than forms related to any possible monomer. This phenomenon emerged from 3D structure, function, and degradation properties of distinctin, a heterodimeric antimicrobial compound consisting of two peptide chains linked by a disulfide bond. After homodimerization in water, this peptide exhibited a fold consisting of a symmetrical full-parallel four-helix bundle, with a well secluded hydrophobic core and exposed basic residues. This fold significantly stabilizes distinctin against proteases compared with other linear amphipathic peptides, without affecting its antimicrobial, hemolytic, and ion-channel formation properties after membrane interaction. This full-parallel helical orientation represents a perfect compromise between formation of a stable structure in water and requirement of a drastic structural rearrangement in membranes to elicit antimicrobial potential. Thus, distinctin can be claimed as a prototype of a previously unrecognized class of antimicrobial derivatives. These results suggest a critical revision of the role of peptide oligomerization whenever solubility or resistance to proteases is known to affect biological properties.NMR structure ͉ oligomerization ͉ pore-forming peptide ͉ disulfide

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Section: Resultssupporting

confidence: 89%

mentioning

confidence: 99%

A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin

Raimondo

Andreotti

Saint

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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“…plicatamide from Styela plicata; styelins (Lee, et al, 1997b) clavanins (Lee at al., 1997a) from Styela clava; Halocynthia aurantium has an array of antimicrobial peptides, inluding halocidin (Jang, et al, 2002), dicynthaurin (Lee, et al, 2001), halocynthin and papillosin (Galinier, et al, 2008); and the peptide named Ci-MAM-A24 has been characterized from Ciona intestinalis (Fedders, et al, 2008).…”

Section: Discussionmentioning

confidence: 99%

“…Halocynthia aurantium are also intermediate in structure: Dicynthaurin is alpha-helical and forms homo-dimers with another molecule of dicynthaurin via a single cysteine present in each molecule (Lee, et al, 2001). Halocidin follows this pattern of helical peptides with a single cysteine forming intermolecular disulphide bridges except that it forms heterodimers between the 15-mers and 18-mers of halocidin (Jang, et al, 2002).…”

Section: Discussionmentioning

confidence: 99%

“…Expanded polyps were anesthetized with magnesium chloride, fixatives (4% v/v paraformaldehyde and 2% v/v glutaraldehyde, both from Ted Pella, Redding, CA) were added drop-wise away from the tissue, and the tissue was fixed overnight at room temperature. Tissue was processed essentially as in Menzel, et al, 2001 Sections were cut parallel to the axial skeleton or perpendicular to the axial skeleton from different blocks. Two to three sections were collected on each grid, three grids worth of sections were collected per block sectioned, and three blocks per orientation were sectioned, stained, and viewed.…”

Section: Transmission Electron Microscopymentioning

confidence: 99%

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Aspects of the Innate Immune System in the Caribbean Octocoral Swiftia exserta

Menzel¹

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All rights reserved.iv ACKNOWLEDGMENTS I wish to thank the members of my committee for their support, patience, and good humor during some very trying times. They selflessly shared reagents, protocols, equipment, and advice; their help has been most appreciated. Using Swiftia exserta, an azooxanthellate ahermatypic local octocoral, as a proxy model organism to study aspects of innate immunity in corals and cnidaria allows us to address both of the reasons listed above while not using endangered species. Utilizing a coral that does not contain symbiotic dinoflagellates (zooxanthellae) simplifies the system by restricting the source of proteins to a single genome. The lack of zooxanthellae in Swiftia exserta also allows the animal's simple adaptation to lab settings.This study of the innate immune system of an octocoral demonstrates: 1) a novel understanding of the microanatomy of octocoral tissues; 2) that Swiftia exserta has at least two cell types that function as constitutive immunocytes; and 3) the presence of two vi potent antibacterial peptides, one with a mass between 4694 and 4696 Daltons. My report on the microanatomy of the coenenchyme, the tissue between polyps, advances the understanding of octocoral anatomy by systematically comparing histology sections with electron micrographs. Applying various techniques of enzyme histochemistry, coupled with cryo-preservation, to the coenenchyme I have identified at least two populations of constitutive immunocytes in Swiftia exserta. Two antibacterial proteins are identified by protein purification and antimicrobial testing techniques. The more active protein is partially characterized with modern hyphenated mass-spectrometry techniques, and can be the focus of future study.

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Antimicrobial Peptides and their Potential as Therapeutants in Aquaculture

Douglas¹

2011

Aquaculture Biotechnology

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Dicynthaurin: an antimicrobial peptide from hemocytes of the solitary tunicate, Halocynthia aurantium

Cited by 86 publications

References 35 publications

A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin

A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin

Aspects of the Innate Immune System in the Caribbean Octocoral Swiftia exserta

Antimicrobial Peptides and their Potential as Therapeutants in Aquaculture

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