Linked Life Data

10880984

Source:http://linkedlifedata.com/resource/pubmed/id/10880984

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
2000-9-7
pubmed:abstractText
A 32-residue peptide, named dermatoxin, has been extracted from the skin of a single specimen of the tree frog Phyllomedusa bicolor, and purified to homogeneity using a four-step protocol. Mass spectral analysis and sequencing of the purified peptide, as well as chemical synthesis and cDNA analysis were consistent with the structure: SLGSFLKGVGTTLASVGKVVSDQF GKLLQAGQ. This peptide proved to be bactericidal towards mollicutes (wall-less eubacteria) and Gram-positive eubacteria, and also, though to a lesser extent, towards Gram-negative eubacteria. Measurement of the bacterial membrane potential revealed that the plasma membrane is the primary target of dermatoxin. Observation of bacterial cells using reflected light fluorescence microscopy after DNA-staining was consistent with a mechanism of cell killing based upon the alteration of membrane permeability rather than membrane solubilization, very likely by forming ion-conducting channels through the plasma membrane. CD spectroscopy and secondary structure predictions indicated that dermatoxin assumes an amphipathic alpha-helical conformation in low polarity media which mimic the lipophilicity of the membrane of target microorganisms. PCR analysis coupled with cDNA cloning and sequencing revealed that dermatoxin is expressed in the skin, the intestine and the brain. Preprodermatoxin from the brain and the intestine have the same sequence as the skin preproform except for two amino-acid substitutions in the preproregion of the brain precursor. The dermatoxin precursor displayed the characteristic features of preprodermaseptins, a family of peptide precursors found in the skin of Phyllomedusa ssp. Precursors of this family have a common N-terminal preproregion followed by markedly different C-terminal domains that give rise to 19-34-residue peptide antibiotics named dermaseptins B and phylloxin, and to the D-amino-acid-containing opioid heptapeptides dermorphins and deltorphins. Because the structures and cidal mechanisms of dermatoxin, dermaseptins B and phylloxin are very different, dermatoxin extends the repertoire of structurally and functionally diverse peptides derived from the rapidly evolving C-terminal domains of precursors of the dermaseptins family.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4583-92
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed-meshheading:10880984-Alamethicin, pubmed-meshheading:10880984-Amino Acid Sequence, pubmed-meshheading:10880984-Amphibian Proteins, pubmed-meshheading:10880984-Animals, pubmed-meshheading:10880984-Anti-Bacterial Agents, pubmed-meshheading:10880984-Antimicrobial Cationic Peptides, pubmed-meshheading:10880984-Bacteria, pubmed-meshheading:10880984-Bufonidae, pubmed-meshheading:10880984-Chromatography, High Pressure Liquid, pubmed-meshheading:10880984-Circular Dichroism, pubmed-meshheading:10880984-Cloning, Molecular, pubmed-meshheading:10880984-Dermotoxins, pubmed-meshheading:10880984-Epidermis, pubmed-meshheading:10880984-Mass Spectrometry, pubmed-meshheading:10880984-Molecular Sequence Data, pubmed-meshheading:10880984-Multigene Family, pubmed-meshheading:10880984-Peptides, pubmed-meshheading:10880984-Protein Structure, Secondary, pubmed-meshheading:10880984-RNA, Messenger, pubmed-meshheading:10880984-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:10880984-Sequence Homology, Amino Acid, pubmed-meshheading:10880984-Spiroplasma, pubmed-meshheading:10880984-Subcellular Fractions, pubmed-meshheading:10880984-Time Factors, pubmed-meshheading:10880984-Tissue Distribution
pubmed:year
2000
pubmed:articleTitle
Isolation of dermatoxin from frog skin, an antibacterial peptide encoded by a novel member of the dermaseptin genes family.
pubmed:affiliation
Laboratoire de Bioactivation des Peptides, Institut Jacques Monod, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't