Home ScanProsite ProRule Documents Downloads Links Funding
	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.

            +----------------------------+
            |                            |
         xxxCxxxxxxxxxxxxxxCxxxCxxxxxxxxxCxxxxxCxCxx
                           |   |               | |
                           +---|---------------+ |
                               +-----------------+

'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.

Note:

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.

Note:

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.

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

INVERT_DEFENSINS, PS51378; Invertebrate defensins family profile  (MATRIX)

• Sequences in UniProtKB/Swiss-Prot known to belong to this class: 51
  • detected by PS51378: 47 (true positives)
  • undetected by PS51378: 4 (4 false negatives and 0 'partial')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS51378:
  NONE.
• Domain architecture view of Swiss-Prot proteins matching PS51378
  
• Retrieve an alignment of UniProtKB/Swiss-Prot true positive hits:
  Clustal format, color, condensed view  /  Clustal format, color  /  Clustal format, plain text  /  Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS51378
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS51378
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS51378
• View ligand binding statistics of PS51378
• Matching PDB structures: 1FJN 1I2U 1I2V 1ICA ... [ALL]

1	Authors	Lambert J., Keppi E., Dimarcq J.-L., Wicker C., Reichhart J.-M., Dunbar B., Lepage P., Van Dorsselaer A., Hoffmann J., Fothergill J.
	Title	Insect immunity: isolation from immune blood of the dipteran Phormia terranovae of two insect antibacterial peptides with sequence homology to rabbit lung macrophage bactericidal peptides.
	Source	Proc. Natl. Acad. Sci. U.S.A. 86:262-266(1989).
	PubMed ID	2911573

2	Authors	Fujiwara S., Imai J., Fujiwara M., Yaeshima T., Kawashima T., Kobayashi K.
	Title	A potent antibacterial protein in royal jelly. Purification and determination of the primary structure of royalisin.
	Source	J. Biol. Chem. 265:11333-11337(1990).
	PubMed ID	2358464

3	Authors	Yamada K., Natori S.
	Title	Purification, sequence and antibacterial activity of two novel sapecin homologues from Sarcophaga embryonic cells: similarity of sapecin B to charybdotoxin.
	Source	Biochem. J. 291:275-279(1993).
	PubMed ID	8471044

4	Authors	Bulet P., Cociancich S., Dimarcq J.-L., Lambert J., Reichhart J.-M., Hoffmann D., Hetru C., Hoffmann J.A.
	Title	Insect immunity. Isolation from a coleopteran insect of a novel inducible antibacterial peptide and of new members of the insect defensin family.
	Source	J. Biol. Chem. 266:24520-24525(1991).
	PubMed ID	1761552

5	Authors	Bulet P., Cociancich S., Reuland M., Sauber F., Bischoff R., Hegy G., Van Dorsselaer A., Hetru C., Hoffmann J.A.
	Title	A novel insect defensin mediates the inducible antibacterial activity in larvae of the dragonfly Aeschna cyanea (Paleoptera, Odonata).
	Source	Eur. J. Biochem. 209:977-984(1992).
	PubMed ID	1425705

6	Authors	Cociancich S., Dupont A., Hegy G., Lanot R., Holder F., Hetru C., Hoffmann J.A., Bulet P.
	Title	Novel inducible antibacterial peptides from a hemipteran insect, the sap-sucking bug Pyrrhocoris apterus.
	Source	Biochem. J. 300:567-575(1994).
	PubMed ID	8002963

7	Authors	Cociancich S., Goyffon M., Bontems F., Bulet P., Bouet F., Menez A., Hoffmann J.
	Title	Purification and characterization of a scorpion defensin, a 4kDa antibacterial peptide presenting structural similarities with insect defensins and scorpion toxins.
	Source	Biochem. Biophys. Res. Commun. 194:17-22(1993).
	PubMed ID	8333834

8	Authors	Lamberty M., Ades S., Uttenweiler-Joseph S., Brookhart G., Bushey D., Hoffmann J.A., Bulet P.
	Title	Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity.
	Source	J. Biol. Chem. 274:9320-9326(1999).
	PubMed ID	10092609

9	Authors	Gueguen Y., Herpin A., Aumelas A., Garnier J., Fievet J., Escoubas J.M., Bulet P., Gonzalez M., Lelong C., Favrel P., Bachere E.
	Title	Characterization of a defensin from the oyster Crassostrea gigas. Recombinant production, folding, solution structure, antimicrobial activities, and gene expression.
	Source	J. Biol. Chem. 281:313-323(2006).
	PubMed ID	16246846
	DOI	10.1074/jbc.M510850200

10	Authors	Mygind 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.
	Title	Plectasin is a peptide antibiotic with therapeutic potential from a saprophytic fungus.
	Source	Nature 437:975-980(2005).
	PubMed ID	16222292
	DOI	10.1038/nature04051

11	Authors	Hanzawa H., Shimada I., Kuzuhara T., Komano H., Kohda D., Inagaki F., Natori S., Arata Y.
	Title	1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin.
	Source	FEBS Lett. 269:413-420(1990).
	PubMed ID	2401368

PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to

Prosite License or see: prosite_license.html.


View entry in original PROSITE document format
View entry in raw text format (no links)