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.
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.
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References
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.
Purification, sequence and antibacterial activity of two novel sapecin homologues from Sarcophaga embryonic cells: similarity of sapecin B to charybdotoxin.
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.
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.
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.
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