1. Molecular cloning of a bombinin gene from Bombina orientalis: detection of NF-kappaB and NF-IL6 binding sites in its promoter
R Miele, D Ponti, H G Boman, D Barra, M Simmaco FEBS Lett. 1998 Jul 10;431(1):23-8. doi: 10.1016/s0014-5793(98)00718-2.
The sequence of a gene from Bombina orientalis was determined which codes for antibacterial peptides. The gene comprises two exons separated by a large intron. Exon 1 codes for the signal peptide, while exon 2 contains the genetic information for two identical bombinins and one bombinin H. The promoter region of the bombinin gene contains putative recognition sites for nuclear factors, such as NFkappaB and NF-IL6. In vivo experiments on B. orientalis have shown that a short contact with bacteria is sufficient to induce a marked increase in the amount of antibacterial peptides in the skin secretion of frogs. This increase was suppressed by pretreatment with glucocorticoids. In the latter case, a significant increase of I kappaB alpha in the secretion is also detectable.
2. Hylins: bombinins H structurally related peptides from the skin secretion of the Brazilian tree-frog Hyla biobeba
Mariana S Castro, Rubens H Matsushita, Antonio Sebben, Marcelo V Sousa, Wagner Fontes Protein Pept Lett. 2005 Jan;12(1):89-93. doi: 10.2174/0929866053405977.
Two hemolytic peptides were isolated from the skin secretion of the Brazilian Hylidae frog Hyla biobeba, using reversed-phase chromatographic procedures. Hylins b1 and b2 exhibit short linear polypeptide chains, a large number of hydrophobic residues, amidated C termini and hemolytic properties. These two novel peptides are the first examples of bombinins H-like peptides isolated from anurans species not related to Bombina species.
