Loading…
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....
Saved in:
Published in: | FEBS letters 1994-04, Vol.342 (3), p.281-285 |
---|---|
Main Authors: | , , , , , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
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 |