Cloning of cDNAs encoding new peptides of the dermaseptin-family.
Dermaseptins are a group of basic (lysine-rich) peptides, 27-34 amino acids in length and involved in the defense of frog skin against microbial invasion. By using a degenerated oligonucleotide primer binding to the 5'-untranslated region of previously characterized cDNAs of these peptides, it was possible to identify new members of the dermaseptin family in the South American frogs Agalychnis annae and Pachymedusa dacnicolor. Amino acid alignment and secondary structure prediction reveals, that only five of the deduced peptides can be supposed to be also functional homologs to the known dermaseptins from Phyllomedusa bicolor and Phyllomedusa sauvagei. The remaining six peptides described in this paper have not been isolated and characterized yet.
Wechselberger
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Institute of Molecular Biology, Austrian Academy of Sciences, Department of Biochemistry, Billrothstr. 11, 5020-Salzburg, Austria. wechselc@1tiblp.nci.nih.gov
D020121:5' Untranslated Regions; D000595:Amino Acid Sequence; D029845:Amphibian Proteins; D000818:Animals; D023181:Antimicrobial Cationic Peptides; D001001:Anura; D017931:DNA Primers; D018076:DNA, Complementary / Q000235:genetics*; D008969:Molecular Sequence Data; D010375:Pedigree; D010455:Peptides / Q000235:genetics*; D013020:South America
D020121:5' Untranslated Regions; D029845:Amphibian Proteins; D023181:Antimicrobial Cationic Peptides; D017931:DNA Primers; D018076:DNA, Complementary; D010455:Peptides; C070905:dermaseptin