• • DRAMP ID

  • DRAMP01549

• • Peptide Name

  • Caerin-1.1 (Frogs, amphibians, animals)

• • Source

  • Litoria splendida (Magnificent tree frog) (Litoria gilleni) (Litoria caerulea)

• • Family

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

• • Gene

  • Not found

• • Sequence

  • GLLSVLGSVAKHVLPHVVPVIAEHL

• • Sequence Length

  • 25

• • UniProt Entry

  • P62568,P62569,Q800R2,P56226

• • Protein Existence

  • Protein level

• • Biological Activity

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

• • Target Organism

  • • [Ref.15203252]Gram-positive bacteria: Bacillus cereus (MIC=50 µg/ml), Leuconostoc lactis (MIC=1.5 µg/ml), Listeria innocua (MIC=25 µg/ml), Micrococcus luteus (MIC=12.5 µg/ml), Staphylococcus aureus (MIC=3-12 µg/ml), Staphylococcus epidermis (MIC=12.5 µg/ml), Streptococcus uberis (MIC=12.5 µg/ml);
    • Gram-negative bacterium: Pasteurella multocida (MIC=25 µg/ml).
    • [Ref.16140737]Virus:HIV:inhibit 50% of PBS-treated HIV infection of T cells(IC50=7.8 μM);inhibition of HIV transfer by dendritic cells to T cells(IC50=12.6 μM)

• • Hemolytic Activity

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

• • Cytotoxicity

  • No cytotoxicity information found in the reference(s) presented

• • Binding Target

  • Cell membrane

• • Linear/Cyclic

  • Linear

• • N-terminal Modification

  • Free

• • C-terminal Modification

  • Amidation

• • Nonterminal Modifications and Unusual Amino Acids

  • Free

• • Stereochemistry

  • L

• • Structure

  • Alpha helix

• • Structure Description

  • The peptide adopts two well-defined helices from Leu2 to Lys11 and from Val17 to His24 separated by a region of less-defined helicity and greater flexibility.

• • Helical Wheel Diagram

  • 

• • PDB ID

  • None

• Predicted Structure

• There is no predicted structure for DRAMP01549.

DRAMP01549

• • Function

  • Antibacterial and antiviral peptides that adopt an alpha helical conformation which can disrupt bacterial membranes. Each caerin displays a different antimicrobial specificity.

• • Tissue specificity

  • Secreted by the skin parotoid and/or rostral glands.

• • Domain

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

• • Miscellaneous

  • Caerin 1.1 completely inhibits 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)

• • PTM

  • C-terminal amidation.

• ·Literature 1

• • 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 2

• • Title

  • The solution structure and activity of caerin 1.1, an antimicrobial peptide from the Australian green tree frog, Litoria splendida.

• • Pubmed ID

  • 9266696

• • Reference

  • Eur J Biochem. 1997 Jul 15;247(2):545-557.

• • Author

  • Wong H, Bowie JH, Carver JA.

• ·Literature 3

• • Title

  • Antimicrobial peptides from hylid and ranin frogs originated from a 150-million-year-old ancestral precursor with a conserved signal peptide but a hypermutable antimicrobial domain.

• • Pubmed ID

  • 12709067

• • Reference

  • Eur J Biochem. 2003 May;270(9):2068-2081.

• • Author

  • Vanhoye D, Bruston F, Nicolas P, Amiche M.

• ·Literature 4

• • 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.