PROSITE documentation PDOC00242
Mammalian defensins signature


Defensins [1,2,3,4,5], also known as α-defensins, are a family of structurally related cysteine-rich peptides active against many Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses. Some defensins are also called corticostatins (CS) because they inhibit corticotropin-stimulated corticosteroid production. Defensins kills cells by forming voltage-regulated multimeric channels in the susceptible cell's membrane. They play a significant role in innate immunity to infection and neoplasia. The peptides known to belong to this family are listed below.

  • Rabbit defensins and corticostatins: CS-I (NP-3A), CS-II (NP-3B), CS-III (MCP-1), CS-IV (MCP-2), NP-4, and NP-5.
  • Guinea-pig neutrophil defensin (GPNP).
  • Human neutrophil defensins 1 to 4 and intestinal defensins 5 and 6.
  • Mouse small bowel cryptdins 1 to 5.
  • Rat NP-1 to NP-4.

All these peptides range in length from 29 to 35 amino acids. There are seven invariant residues, including six cysteines all involved in intrachain disulfide bonds. A schematic representation of peptides from the defensin family is shown below.

                    |     |         |         |
                    +-----|---------+         |
'C': conserved cysteine involved in a disulfide bond.
'*': position of the pattern.

Our pattern is based on the conserved residues.

Last update:

May 2004 / Text revised.


Technical section

PROSITE method (with tools and information) covered by this documentation:

DEFENSIN, PS00269; Mammalian defensins signature  (PATTERN)


1AuthorsLehrer R.I. Ganz T. Selsted M.E.
SourceASM News 56:315-318(1990).

2AuthorsLehrer R.I. Ganz T. Selsted M.E.
TitleDefensins: endogenous antibiotic peptides of animal cells.
SourceCell 64:229-230(1991).
PubMed ID1988144

3AuthorsKagan B.L. Ganz T. Lehrer R.I.
TitleDefensins: a family of antimicrobial and cytotoxic peptides.
SourceToxicology 87:131-149(1994).
PubMed ID7512758

4AuthorsLehrer R.I. Lichtenstein A.K. Ganz T.
TitleDefensins: antimicrobial and cytotoxic peptides of mammalian cells.
SourceAnnu. Rev. Immunol. 11:105-128(1993).
PubMed ID8476558

5AuthorsWhite S.H. Wimley W.C. Selsted M.E.
TitleStructure, function, and membrane integration of defensins.
SourceCurr. Opin. Struct. Biol. 5:521-527(1995).
PubMed ID8528769

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