Primary structure and cellular localization of callinectin, an antimicrobial peptide from the blue crab.
Dev Comp Immunol
; 35(4): 409-15, 2011 Apr.
Article
en En
| MEDLINE
| ID: mdl-21115038
ABSTRACT
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.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Braquiuros
/
Péptidos Catiónicos Antimicrobianos
Límite:
Animals
Idioma:
En
Revista:
Dev Comp Immunol
Año:
2011
Tipo del documento:
Article
País de afiliación:
Estados Unidos