Cecropin

Cecropin family
Model of Drosophila melanogaster Cecropin A
Identifiers
SymbolCecropin
PfamPF00272
InterProIPR000875
PROSITEPDOC00241
SCOP21f0d / SCOPe / SUPFAM
TCDB1.C.17
OPM superfamily151
OPM protein1d9j
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Cecropins are antimicrobial peptides.[1][2] They were first isolated from the hemolymph of Hyalophora cecropia, whence the term cecropin was derived. Cecropins lyse bacterial cell membranes; they also inhibit proline uptake and cause leaky membranes.

Cecropins[3][4][5] constitute a main part of the innate immune system of insects. Cecropins are small proteins anywhere from 31 - 37 amino acids long and are active against both gram-positive and gram-negative bacteria. Cecropins isolated from insects other than Hyalophora cecropia (Cecropia moth) have been given various names, such as bactericidin, lepidopterin, and sarcotoxin. All of these peptides are structurally related.

  1. ^ Cecropins at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
  2. ^ Lauwers A, Twyffels L, Soin R, Wauquier C, Kruys V, Gueydan C (March 2009). "Post-transcriptional Regulation of Genes Encoding Anti-microbial Peptides in Drosophila". The Journal of Biological Chemistry. 284 (13): 8973–83. doi:10.1074/jbc.M806778200. PMC 2659254. PMID 19176529.
  3. ^ Boman HG, Hultmark D (1987). "Cell-free immunity in insects". Annual Review of Microbiology. 41: 103–26. doi:10.1146/annurev.mi.41.100187.000535. PMID 3318666.
  4. ^ Boman HG (April 1991). "Antibacterial peptides: key components needed in immunity". Cell. 65 (2): 205–7. doi:10.1016/0092-8674(91)90154-Q. PMID 2015623. S2CID 42206617.
  5. ^ Boman HG, Faye I, Gudmundsson GH, Lee JY, Lidholm DA (October 1991). "Cell-free immunity in Cecropia. A model system for antibacterial proteins". European Journal of Biochemistry. 201 (1): 23–31. doi:10.1111/j.1432-1033.1991.tb16252.x. PMID 1915368.