PROSITE documentation PDOC00356
Invertebrate defensins family profile


Invertebrate defensins are a family of cysteine-rich antimicrobial peptides, primarily active against Gram-positive bacteria. These defensins have been found in arthropods (insects, ticks, spiders and scorpions), in bivalve molluscs and in a fungus. These peptides range in length from 32 to 51 amino acids. There are six conserved cysteines all involved in intrachain disulfide bonds. A schematic representation of peptides from the invertebrate defensin family is shown below.

            |                            |
                           |   |               | |
                           +---|---------------+ |
'C': conserved cysteine involved in a disulfide bond.

Some peptides known to belong to this family are listed below.

  • Phormicin A and B from black blowfly (Phormia terranovae) [1].
  • Royalisin from the royal jelly of honey bee [2].
  • Sapecin, sapecin B and sapecin C from flesh fly (Sarcophaga peregrina) [3].
  • Antibacterial peptides B and C from the beetle Zophobas atratus [4].
  • Defensin from the larva of the dragonfly Aeschna cyanea [5].
  • Defensin from Pyrrhocoris apterus [6].
  • 4 Kd defensin from the scorpion Leiurus quinquestriatus hebraeus [7].
  • Defensin heliomicin from the larva, tobacco budworm, of Heliothis virescens with potent anti-fungal activity [8].
  • Defensins from mussels (Mytilus edulis and M. galloprovincialis).
  • Defensin from oyster (Crassostrea virginica) [9].
  • Plectasin from a saprophytic fungus (Pseudoplectania nigrella) [10].

We developed a profile that covers the whole structure of invertebrate defensins.


Although low level sequence similarities have been reported [1] between the invertebrate defensins and mammalian defensins, the topological arrangement of the disulfide bonds as well as the tertiary structure [11] are completely different in the two families.


Because historically these defensins were first found in insects and scorpions, they used to be called arthropod defensin family or insect defensins.

Last update:

May 2008 / Pattern removed, profile added and text revised.


Technical section

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

INVERT_DEFENSINS, PS51378; Invertebrate defensins family profile  (MATRIX)


1AuthorsLambert J. Keppi E. Dimarcq J.-L. Wicker C. Reichhart J.-M. Dunbar B. Lepage P. Van Dorsselaer A. Hoffmann J. Fothergill J.
TitleInsect immunity: isolation from immune blood of the dipteran Phormia terranovae of two insect antibacterial peptides with sequence homology to rabbit lung macrophage bactericidal peptides.
SourceProc. Natl. Acad. Sci. U.S.A. 86:262-266(1989).
PubMed ID2911573

2AuthorsFujiwara S. Imai J. Fujiwara M. Yaeshima T. Kawashima T. Kobayashi K.
TitleA potent antibacterial protein in royal jelly. Purification and determination of the primary structure of royalisin.
SourceJ. Biol. Chem. 265:11333-11337(1990).
PubMed ID2358464

3AuthorsYamada K. Natori S.
TitlePurification, sequence and antibacterial activity of two novel sapecin homologues from Sarcophaga embryonic cells: similarity of sapecin B to charybdotoxin.
SourceBiochem. J. 291:275-279(1993).
PubMed ID8471044

4AuthorsBulet P. Cociancich S. Dimarcq J.-L. Lambert J. Reichhart J.-M. Hoffmann D. Hetru C. Hoffmann J.A.
TitleInsect immunity. Isolation from a coleopteran insect of a novel inducible antibacterial peptide and of new members of the insect defensin family.
SourceJ. Biol. Chem. 266:24520-24525(1991).
PubMed ID1761552

5AuthorsBulet P. Cociancich S. Reuland M. Sauber F. Bischoff R. Hegy G. Van Dorsselaer A. Hetru C. Hoffmann J.A.
TitleA novel insect defensin mediates the inducible antibacterial activity in larvae of the dragonfly Aeschna cyanea (Paleoptera, Odonata).
SourceEur. J. Biochem. 209:977-984(1992).
PubMed ID1425705

6AuthorsCociancich S. Dupont A. Hegy G. Lanot R. Holder F. Hetru C. Hoffmann J.A. Bulet P.
TitleNovel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus.
SourceBiochem. J. 300:567-575(1994).
PubMed ID8002963

7AuthorsCociancich S. Goyffon M. Bontems F. Bulet P. Bouet F. Menez A. Hoffmann J.
TitlePurification and characterization of a scorpion defensin, a 4kDa antibacterial peptide presenting structural similarities with insect defensins and scorpion toxins.
SourceBiochem. Biophys. Res. Commun. 194:17-22(1993).
PubMed ID8333834

8AuthorsLamberty M. Ades S. Uttenweiler-Joseph S. Brookhart G. Bushey D. Hoffmann J.A. Bulet P.
TitleInsect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity.
SourceJ. Biol. Chem. 274:9320-9326(1999).
PubMed ID10092609

9AuthorsGueguen Y. Herpin A. Aumelas A. Garnier J. Fievet J. Escoubas J.M. Bulet P. Gonzalez M. Lelong C. Favrel P. Bachere E.
TitleCharacterization of a defensin from the oyster Crassostrea gigas. Recombinant production, folding, solution structure, antimicrobial activities, and gene expression.
SourceJ. Biol. Chem. 281:313-323(2006).
PubMed ID16246846

10AuthorsMygind P.H. Fischer R.L. Schnorr K.M. Hansen M.T. Sonksen C.P. Ludvigsen S. Raventos D. Buskov S. Christensen B. De Maria L. Taboureau O. Yaver D. Elvig-Jorgensen S.G. Sorensen M.V. Christensen B.E. Kjaerulff S. Frimodt-Moller N. Lehrer R.I. Zasloff M. Kristensen H.H.
TitlePlectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus.
SourceNature 437:975-980(2005).
PubMed ID16222292

11AuthorsHanzawa H. Shimada I. Kuzuhara T. Komano H. Kohda D. Inagaki F. Natori S. Arata Y.
Title1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin.
SourceFEBS Lett. 269:413-420(1990).
PubMed ID2401368

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