Primary structure and cellular localization of callinectin, an antimicrobial peptide from the blue crab Public Deposited
- Creator
- Noga, Edward J.
- Stone, Kathryn L.
- Wood, Abbey
- Gordon, William L.
- Robinette, David
- Abstract
- We report the complete amino acid sequence of callinectin, a 32 amino acid, proline-, arginine-rich 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 immunoelectron 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.
- Date of publication
- 2011
- Keyword
- DOI
- Identifier
- PMCID: PMC3046215
- Publisher DOI: https://doi.org/10.1016/j.dci.2010.11.015
- PMID: 21115038
- Onescience id: faffc177aaac07015874a09a03bccd4039f70f4b
- Resource type
- Article
- Rights statement
- In Copyright
- Journal title
- Developmental and Comparative Immunology
- Journal volume
- 35
- Journal issue
- 4
- Page start
- 409
- Page end
- 415
- Language
- English
- ISSN
- 1879-0089
- 0145-305X
- Parents:
This work has no parents.
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