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Gallinacins: cysteine-rich antimicrobial peptides of chicken leukocytes

We purified three homologous antimicrobial peptides (‘gallinacins’) from chicken leukocytes, examined their antimicrobial activity in vitro, and established their primary sequences by a combination of gas phase microsequencing and on-line LC-ESI-MS analysis of endo- and exoprotease peptide digests....

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Bibliographic Details
Published in:FEBS letters 1994-04, Vol.342 (3), p.281-285
Main Authors: Harwig, Sylvia S.L., Swiderek, Kristine M., Kokryakov, Vladimir N., Tan, Leonie, Lee, Terry D., Panyutich, Elena A., Aleshina, Galina M., Shamova, Olga V., Lehrer, Robert I.
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Language:English
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Summary:We purified three homologous antimicrobial peptides (‘gallinacins’) from chicken leukocytes, examined their antimicrobial activity in vitro, and established their primary sequences by a combination of gas phase microsequencing and on-line LC-ESI-MS analysis of endo- and exoprotease peptide digests. The peptides contained 36–39 amino acid residues, were relatively cationic due to their numerous lysine and arginine residues, and each contained 3 intramolecular cystine disulfide bonds. Gallinacins showed primary sequence homology to the recently delineated β-defensin family, heretofore found only in the respiratory epithelial cells and neutrophils of cattle, suggesting that β-defensins originated at least 250 million years ago, before avian and mammalian lineages diverged. The 9 invariant residues (6 cysteines, 2 glycines and 1 proline) common to avian gallinacins and bovine β-defensins are likely to constitute the essential primary structural motif of this ancient family of host-defense peptides.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(94)80517-2