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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
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Amos Bairoch

PROSITE documentation PDOC00241
Cecropin family signature


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PURL: https://purl.expasy.org/prosite/documentation/PDOC00241

Description

Cecropins [1,2,3] are potent antibacterial proteins that constitute a main part of the cell-free immunity of insects. Cecropins are small proteins of about 35 amino acid residues active against both Gram-positive and Gram-negative bacteria. They seem to exert a lytic action on bacterial membranes.

Cecropins isolated from insects other than Cecropia have been given various names: bactericidin, lepidopteran, sarcotoxin, etc. All of these peptides are structurally related. Cecropin P1, an intestinal antibacterial peptide from pig, also belongs to this family.

As a signature pattern for this family of active peptides, we selected a conserved region in the N-terminal section of cecropins.

Last update:

April 2006 / Pattern revised.

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Technical section

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

CECROPIN, PS00268; Cecropin family signature  (PATTERN)


References

1AuthorsBoman H.G. Hultmark D.
TitleCell-free immunity in insects.
SourceAnnu. Rev. Microbiol. 41:103-126(1987).
PubMed ID3318666
DOI10.1146/annurev.mi.41.100187.000535

2AuthorsBoman H.G.
TitleAntibacterial peptides: key components needed in immunity.
SourceCell 65:205-207(1991).
PubMed ID2015623

3AuthorsBoman H.G. Faye I. Gudmundsson G.H. Lee J.-Y. Lidholm D.A.
TitleCell-free immunity in Cecropia. A model system for antibacterial proteins.
SourceEur. J. Biochem. 201:23-31(1991).
PubMed ID1915368



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