• • DRAMP ID

  • DRAMP03594

• • Peptide Name

  • Neutrophil defensin 4 (Defensin, alpha 4; HNP-4, HP-4; Human, mammals, animals)

• • Source

  • Homo sapiens (Human)

• • Family

  • Belongs to the alpha-defensin family

• • Gene

  • DEFA4

• • Sequence

  • VCSCRLVFCRRTELRVGNCLIGGVSFTYCCTRV

• • Sequence Length

  • 33

• • UniProt Entry

  • P12838

• • Protein Existence

  • Protein level

• • Biological Activity

  • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-, Antifungal, Antiviral(SARS-CoV-2)

• • Target Organism

  • • [Ref.34206990]Virus:showed inhibition against SARS-CoV-2.Gram-negative bacteria: Escherichia coli ATCC 8739 (vLD50=3.3±0.4 µg/ml), E. coli ATCC 25922 (vLD50=3.0±0.7 µg/ml), Enterobacter aerogenes ATCC 13048 (vLD50=6.6±0.2 µg/ml);
    • Gram-positive bacteria: Staphylococcus aureus ATCC 25923 (vLD50=7.3±1.4 µg/ml), S. aureus ATCC 29213 (vLD50=7.2±0.2 µg/ml), Bacillus cereus ATCC 10876 (vLD50=0.87±0.08 µg/ml).(Ref.4)
    • NOTE: vLD50, virtual lethal doses (vLDs), equivalent to conventional 50% lethal doses (LD50s).
    • Yeast: Candida albicans ATCC 99788 amphotericin B resistant (IC90>100 µg/ml).(Ref.2)

• • 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

  • Not found

• • Linear/Cyclic

  • Cyclic

• • N-terminal Modification

  • Free

• • C-terminal Modification

  • Free

• • Nonterminal Modifications and Unusual Amino Acids

  • Disulfide bonds between Cys2 and Cys30,Cys4 and Cys19,Cys9 and Cys29.

• • Stereochemistry

  • L

• • Structure

  • Beta strand

• • Structure Description

  • Compared to HNP-2, HNP-1 contains one additional residue (Ala) at the N-terminus. It contains a long stretch of a double-stranded antiparallel beta-sheet in a hairpin conformation that contains a beta-bulge, a short region of triple-stranded beta-sheet, and several tight turns.

• • Helical Wheel Diagram

  • 

• • PDB ID

  • 1ZMM resolved by X-ray.

• Predicted Structure

• There is no predicted structure for DRAMP03594.

DRAMP03594

• • Function

  • Has antimicrobial activity against Gram-negative bacteria, and to a lesser extent also against Gram-positive bacteria and fungi. Protects blood cells against infection with HIV-1 (in vitro). In comparison with HNP1-3, inhibition of both strains of HIV-1 by HNP4 was noticeably stronger as evidenced by lower IC50 values (2-5 µM) and steeper and more complete inhibition curves.

• • PTM

  • Contains three disulfide bonds 2-30; 4-19; 9-29.

• ·Literature 1

• • Title

  • Human Defensins Inhibit SARS-CoV-2 Infection by Blocking Viral Entry.

• • Pubmed ID

  • 34206990

• • Reference

  • Viruses. 2021 Jun 26;13(7):1246.

• • Author

  • Xu C, Wang A, Marin M, Honnen W, Ramasamy S, Porter E, Subbian S, Pinter A, Melikyan GB, Lu W, Chang TL.

• ·Literature 2

• • Title

  • Crystal structures of human alpha-defensins HNP4, HD5, and HD6.

• • Pubmed ID

  • 17088326

• • Reference

  • Protein Sci. 2006 Dec;15(12):2749-2760.

• • Author

  • Szyk A, Wu Z, Tucker K, Yang D, Lu W, Lubkowski J.

• ·Literature 3

• • Title

  • Human neutrophil alpha-defensin 4 inhibits HIV-1 infection in vitro.

• • Pubmed ID

  • 15620707

• • Reference

  • FEBS Lett. 2005 Jan 3;579(1):162-166.

• • Author

  • Wu Z, Cocchi F, Gentles D, Ericksen B, Lubkowski J, Devico A, Lehrer RI, Lu W.

• ·Literature 4

• • Title

  • Antibacterial activity and specificity of the six human {alpha}-defensins.

• • Pubmed ID

  • 15616305

• • Reference

  • Antimicrob Agents Chemother. 2005 Jan;49(1):269-275.

• • Author

  • Ericksen B, Wu Z, Lu W, Lehrer RI.