Journal
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
Volume 35, Issue 4, Pages 409-415Publisher
ELSEVIER SCI LTD
DOI: 10.1016/j.dci.2010.11.015
Keywords
Antimicrobial peptide; Cystine; Proline; Arginine; Hydroxylated tryptophan
Categories
Funding
- Fishery Research Grant Project [99-AM-01]
- Blue Crab Research Project [03-BIOL-01, 06-Biol-01]
- U.S.D.A. Agriculture and Food Research [2009-03571]
- Yale School of Medicine's Clinical and Translational Science (CTSA) [UL1 R024139]
- National Center for Research Resources, National Institutes of Health
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We report the complete amino acid sequence of callinectin, a 32 amino acid, proline-, arginine-rich antimicrobial peptide (AMP) with four cysteines and having the sequence WNSNRRFRVGRPPVVGRPGCVCFRAPCPCSNY-amide. The primary structure of callinectin is highly similar to arasins, AMPs recently identified in the small spider crab (Hyas araneus). Callinectin exists in three isomers that vary in the functional group on the tryptophan (W)residue. The most prevalent isomer had a hydroxy-N-formylkynurenine group, while the other two isomers had either N-formylkynurenine or hydroxy-tryptophan. Using a sequence highly similar to native callinectin, we chemically synthesized a peptide which we called callinectin-like peptide (CLP). Via immuno-electron microscopy, affinity-purified rabbit antibodies raised to CLP successfully localized the site of callinectin in blue crab hemocytes to the large electron-dense granules that are found primarily in large granule hemocytes. (C) 2010 Elsevier Ltd. All rights reserved.
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