• • DRAMP ID

  • DRAMP02768

• • Peptide Name

  • Pilosulin-1 (Myr b I; ants, insects, animals)

• • Source

  • Myrmecia banksi (Jack jumper ant) (Australian jumper ant)

• • Family

  • Belongs to the pilosulin family

• • Gene

  • Not found

• • Sequence

  • GLGSVFGRLARILGRVIPKVAKKLGPKVAKVLPKVMKEAIPMAVEMAKSQEEQQPQ

• • Sequence Length

  • 56

• • UniProt Entry

  • Q07932,Q9TWC1

• • Protein Existence

  • Protein level

• • Biological Activity

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

• • Target Organism

  • • [Ref.9813247]Gram-positive bacteria: Micrococcus luteus (MIC=0.5 µM), Enterococcus spp.I-11305b (MIC=2 µM), Enterococcus spp. I-11054 (MIC=2 µM), Staphylococcus simulans 22 (MIC=2 µM), S. haemolyticus I-10925 (MIC=2 µM), S. epidermidis LT1324 (MIC=2 µM), S. aureuss 5185 (MI=2 µM), S. aureuss methicillin-sensitive I-11574 (MIC=2 µM), S. aureuss (MRSA) LT1338 (MIC=3 µM), S. aureuss (MRSA) LT1334 (MIC=1.5 µM);
    • Gram-negative bacteria: Citrobacter freundii I-11090 (MIC=2 µM), Klebsiella pneumoniae I-10910 (MIC=2 µM), Escherichia coli I-11276b (MIC=4 µM), E. coli O-19592 (MIC=2 µM), Stenotrophomonas maltophilia O-16451 (MIC=2 µM), S. maltophila I-10717 (MIC=2 µM), Pseudomonas aeruginosa 4991 (MIC=4 µM), Pseudomonas aeruginosa I-10968 (MIC=4 µM);
    • Fungi: Candida albicans I-11301 (MIC=4 µM), Candida albicans I-11134 (MIC>4 µM).

• • Hemolytic Activity

  • • [Ref.9813247]Complete lysis in the presence of pilosulin 1 was obtained at a concentration of 40 μM with evidence of partial lysis visible down to 1.25 μM

• • Cytotoxicity

  • • Not included yet

• • Binding Target

  • IgE

• • Linear/Cyclic

  • Not included yet

• • N-terminal Modification

  • Not included yet

• • C-terminal Modification

  • Not included yet

• • Nonterminal Modifications and Unusual Amino Acids

  • Not included yet

• • Stereochemistry

  • Not included yet

• • Structure

  • Alpha helix

• • Structure Description

  • Not found

• • Helical Wheel Diagram

  • 

• • PDB ID

  • None

• Predicted Structure

• There is no predicted structure for DRAMP02768.

DRAMP02768

• • Function

  • Has strong cytotoxic and hemolytic activities. Is more potent against mononuclear leukocytes than against granulocytes. The synthesized peptide 57-76 shows a potent and broad spectrum antimicrobial activity against both Gram-positive and Gram-negative bacteria, and also against the fungus C. albicans. Adopts an alpha-helical structure.

• • Tissue specificity

  • Expressed by the venom gland.

• • Allergenic properties

  • Causes an allergic reaction in human.

• ·Literature 1

• • Title

  • Identification and optimization of an antimicrobial peptide from the ant venom toxin pilosulin.

• • Pubmed ID

  • 9813247

• • Reference

  • Arch Biochem Biophys. 2005 Feb 15;434(2):358-364.

• • Author

  • Zelezetsky I, Pag U, Antcheva N, Sahl HG, Tossi A.

• ·Literature 2

• • Title

  • Flow cytometric analysis of cell killing by the jumper ant venom peptide pilosulin 1.

• • Pubmed ID

  • 9701394

• • Reference

  • Cytometry. 1998 Aug 1;32(4):268-273.

• • Author

  • King MA, Wu QX, Donovan GR, Baldo BA.

• ·Literature 3

• • Title

  • Identification and optimization of an antimicrobial peptide from the ant venom toxin pilosulin.

• • Pubmed ID

  • 15639237

• • Reference

  • Arch Biochem Biophys. 2005 Feb 15;434(2):358-364.

• • Author

  • Zelezetsky I, Pag U, Antcheva N, Sahl HG, Tossi A.

• ·Literature 4

• • Title

  • Expression of jumper ant (Myrmecia pilosula) venom allergens: post-translational processing of allergen gene products.

• • Pubmed ID

  • 8866004

• • Reference

  • Biochem Mol Biol Int. 1996 Aug;39(5):877-885.

• • Author

  • Donovan GR, Street MD, Tetaz T, Smith AI, Alewood D, Alewood P, Sutherland SK, Baldo BA.