Antimicrobial peptides in the stomach of Xenopus laevis.

Moore, Kristin J.; Bevins, Charles L.; Brasseur, Michael M.; Tomassini, N; Turner, Kent; Eck, H S; Zasloff, Michael

doi:10.1016/s0021-9258(18)55069-9

Cited by 139 publications

(19 citation statements)

References 51 publications

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“…They contribute to an essential part of the innate immunity of insects and mammals (Boman, 1995). Their primary chemical and structural features are common to other peptide antibiotics like the magainins, isolated from frog skin (Moore et al, 1991), and the defensins (Lehrer et al, 1993). All of these peptides cause the rapid lysis of bacteria in a concentrationdependent manner, display a high degree of primary sequence homology within individual families, contain highly positively charged amphipathic structures, and have a specificity for bacterial cells and acidic phospholipids.…”

Section: Introductionmentioning

confidence: 99%

Orientation of Cecropin A Helices in Phospholipid Bilayers Determined by Solid-State NMR Spectroscopy

Marassi

Opella

Juvvadi

et al. 1999

Biophysical Journal

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The orientation of the insect antibiotic peptide cecropin A (CecA) in the phospholipid bilayer membrane was determined using (15)N solid-state NMR spectroscopy. Two peptide samples, each specifically labeled with (15)N at Val(11) or Ala(27), were synthesized by solid phase techniques. The peptides were incorporated into phospholipid bilayers, prepared from a mixture of dimyristoylphosphatidylcholine and dimyristoylphosphatidylglycerol, and oriented on glass slides. The (15)N chemical shift solid-state NMR spectra from these uniaxially oriented samples display a single (15)N chemical shift frequency for each labeled residue. Both frequencies are near the upfield end of the (15)N chemical shift powder pattern, as expected for an alpha-helix with its long axis in the plane of the membrane and the NH bonds perpendicular to the direction of the magnetic field. These results support a mechanism of action in which CecA binds to and covers the membrane surface, thereby causing a general destabilization and leakiness of the lipid bilayer membrane. The data are discussed in relation to a proposed mechanism of membrane lysis and bacterial killing via an ion channel activity of CecA.

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Section: Introductionmentioning

confidence: 99%

Orientation of Cecropin A Helices in Phospholipid Bilayers Determined by Solid-State NMR Spectroscopy

Marassi

Opella

Juvvadi

et al. 1999

Biophysical Journal

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“…Antibiotic peptides are produced as a barrier against infections and may be constitutively expressed or induced in response to endogenous and/or exogenous stimulations or triggered by microorganisms. Constitutively expressed and neuroendocryn/injury-stimulated peptides such as seminalplasmin and magainins (18,19) are reported more frequently among vertebrates, although in some cases peptides elicited by traumas have been described in insects (20)(21)(22), and a constitutively expressed defensin-like peptide from a scorpion has also been described (23).…”

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confidence: 99%

cDNA Sequence and Expression of the Ceratotoxin Gene Encoding an Antibacterial Sex-specific Peptide from the Medfly Ceratitis capitata (diptera)

Marchini

Manetti

Rosetto³

et al. 1995

Journal of Biological Chemistry

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Ceratotoxins are antibacterial 3-kDa molecular mass amphiphilic peptides isolated from the female reproductive accessory glands of the medfly Ceratitis capitata. They are physiologically related to bee melittin and show amino acid sequence homology with magainin peptides. In this paper, we report the complete sequence of cDNA coding for ceratotoxin A and the expression of the gene during the life cycle of the insect. Experimental data show that the ceratotoxin is a gene expressed exclusively in the imaginal stages and that it is female-specific, related to sexual maturity, and stimulated by mating. Differently from most antibacterial insect hemolymph peptides, it is not induced by microbial infection. Western blot analysis using an anti-ceratotoxin antibody indicates the female accessory glands as the only site where the production of the ceratotoxin peptide occurs.

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“…Peptidomic analysis has been used to identify and characterize multiple peptides belonging to magainin, PGLa, CPF, and XPF families from skin secretions of frogs inhabiting both ranges. In addition, a peptide with limited amino acid sequence similarity to peptide glycine-glutamine (PGQ), previously identified only in an extract of the stomach of X. laevis [32], was isolated from secretions of frogs from both ranges. X. laevis PGQ shows broadspectrum, albeit weak, antimicrobial activity [32].…”

Section: Discussionmentioning

confidence: 99%

“…In addition, a peptide with limited amino acid sequence similarity to peptide glycine-glutamine (PGQ), previously identified only in an extract of the stomach of X. laevis [32], was isolated from secretions of frogs from both ranges. X. laevis PGQ shows broadspectrum, albeit weak, antimicrobial activity [32]. A comparison of the chromatograms of skin secretions of female frogs from the Cape Peninsula (Fig.…”

Section: Discussionmentioning

confidence: 99%

Evidence from peptidomic analysis of skin secretions that allopatric populations of Xenopus gilli (Anura:Pipidae) constitute distinct lineages

Conlon¹,

Mechkarska²,

Coquet³

et al. 2015

Peptides

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The International Union for Conservation of Nature (IUCN) Endangered Cape Platanna Xenopus gilli inhabits disjunct ranges at the tip of Cape Peninsula and near the town of Kleinmond on opposite sides of False Bay in the extreme southwest of Africa. Peptidomic analysis of host-defense peptides in norepinephrine-stimulated skin secretions from frogs from the Cape Peninsula range resulted in the identification of two magainins, two peptide glycine-leucine-amide (PGLa) peptides, two xenopsin-precursor fragment (XPF) peptides, nine caerulein-precursor fragment (CPF) peptides, and a peptide related to peptide glycine-glutamine (PGQ) previously found in an extract of Xenopus laevis stomach. The primary structures of the peptides indicate a close phylogenetic relationship between X. gilli and X. laevis but only magainin-1, PGLa and one CPF peptide are identical in both species. Consistent with previous data, the CPF peptides show the greatest antimicrobial potency but are hemolytic. There are appreciable differences in the expression of host-defense peptide genes in frogs from the population of animals sampled near Kleinmond as peptides corresponding to magainin-G2, XPF-G1, XPF-G2, and four CPF peptides, present in secretions from the Cape Peninsula frogs, were not identified in the skin secretions from Kleinmond frogs. Conversely, PGLa-G3, XPF-G3, and three CPF peptides were identified in the Kleinmond frogs but not in the Cape Peninsula animals. The data support the conclusion from morphometric analyses and comparisons of the nucleotide sequences of mitochondrial genes that the disjunct populations of X. gilli have undergone appreciable genetic, morphological, and phenotypic divergence.

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Antimicrobial peptides in the stomach of Xenopus laevis.

Cited by 139 publications

References 51 publications

Orientation of Cecropin A Helices in Phospholipid Bilayers Determined by Solid-State NMR Spectroscopy

Orientation of Cecropin A Helices in Phospholipid Bilayers Determined by Solid-State NMR Spectroscopy

cDNA Sequence and Expression of the Ceratotoxin Gene Encoding an Antibacterial Sex-specific Peptide from the Medfly Ceratitis capitata (diptera)

Evidence from peptidomic analysis of skin secretions that allopatric populations of Xenopus gilli (Anura:Pipidae) constitute distinct lineages

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