• • DRAMP ID

  • DRAMP01560

• • Peptide Name

  • Caerin-1.9 (Frogs, amphibians, animals)

• • Source

  • Litoria chloris (Blue-thighed frog) (frog skin active peptide family)

• • Family

  • Belongs to the frog skin active peptide family (Caerin subfamily)

• • Gene

  • Not found

• • Sequence

  • GLFGVLGSIAKHVLPHVVPVIAEKL

• • Sequence Length

  • 25

• • UniProt Entry

  • P81252

• • Protein Existence

  • Protein level

• • Biological Activity

  • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral

• • Target Organism

  • • [Ref.15203252]Gram-positive bacteria: Bacillus cereus (MIC=100 µg/ml), Leuconostoc lactis (MIC=12 µg/ml), Listeria innocua (MIC=50 µg/ml), Micrococcus luteus (MIC=50 µg/ml), Staphylococcus aureus (MIC=100 µg/ml), Staphylococcus epidermis (MIC=25 µg/ml), Streptococcus uberis (MIC=50 µg/ml);
    • Gram-negative bacterium: Pasteurella multocida (MIC=50 µg/ml).
    • [Ref.16140737]Virus:HIV:inhibit 50% of PBS-treated HIV infection of T cells(IC50=1.2 μM);inhibition of HIV transfer by dendritic cells to T cells(IC50=1.6 μM).
    • [Ref.26026377]Virus:HIV: inhibition of HIV Pseudovirus (PsV) infection in CD4+ T cells(IC50=4 µM).

• • Hemolytic Activity

  • • No hemolysis information or data found in the reference(s) presented in this entry

• • Cytotoxicity

  • • [Ref.26026377]CD4+ T Lymphocytes:50% cell death at 20 µM.

• • Binding Target

  • Not found

• • Linear/Cyclic

  • Linear

• • N-terminal Modification

  • Free

• • C-terminal Modification

  • Amidation

• • Nonterminal Modifications and Unusual Amino Acids

  • Free

• • Stereochemistry

  • L

• • Structure

  • Not found

• • Structure Description

  • Not found

• • Helical Wheel Diagram

  • 

• • PDB ID

  • None

• Predicted Structure

• There is no predicted structure for DRAMP01560.

DRAMP01560

• • Function

  • Antibacterial peptide, that adopts an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity.

• • Tissue specificity

  • Expressed by the skin dorsal glands.

• • Domain

  • Contains two amphipathic alpha helix regions separated by a region of less-defined helicity and greater flexibility (By similarity).

• • PTM

  • C-terminal amidation.

• • Miscellaneous

  • Caerin 1.9 completely inhibited HIV infection of T cells within minutes of exposure to virus at concentrations that were not toxic to target cells (J Virol. 2005 Sep;79(18)

• ·Literature 1

• • Title

  • Inhibition of HIV infection by caerin 1 antimicrobial peptides.

• • Pubmed ID

  • 26026377

• • Reference

  • Peptides. 2015 Sep;71:296-303.

• • Author

  • VanCompernolle S, Smith PB, Bowie JH, Tyler MJ, Unutmaz D, Rollins-Smith LA.

• ·Literature 2

• • Title

  • Antimicrobial peptides from amphibian skin potently inhibit human immunodeficiency virus infection and transfer of virus from dendritic cells to T cells.

• • Pubmed ID

  • 16140737

• • Reference

  • J Virol. 2005 Sep;79(18):11598-606.

• • Author

  • VanCompernolle SE, Taylor RJ, Oswald-Richter K, Jiang J, Youree BE, Bowie JH, Tyler MJ, Conlon JM, Wade D, Aiken C, Dermody TS, KewalRamani VN, Rollins-Smith LA, Unutmaz D.

• ·Literature 3

• • Title

  • Host-defence peptides of Australian anurans: structure, mechanism of action and evolutionary significance.

• • Pubmed ID

  • 15203252

• • Reference

  • Peptides. 2004 Jun;25(6):1035-1054.

• • Author

  • Apponyi MA, Pukala TL, Brinkworth CS, Maselli VM, Bowie JH, Tyler MJ, Booker GW, Wallace JC, Carver JA, Separovic F, Doyle J, Llewellyn LE.

• ·Literature 4

• • Title

  • New antibiotic caerin 1 peptides from the skin secretion of the Australian tree frog Litoria chloris. Comparison of the activities of the caerin 1 peptides from the genus Litoria.

• • Pubmed ID

  • 9516047

• • Reference

  • J Pept Res. 1998 Feb;51(2):121-126.

• • Author

  • Steinborner ST, Currie GJ, Bowie JH, Wallace JC, Tyler MJ.