New Actinoporins from sea anemone Heteractis crispa: cloning and functional expression.
Biochemistry (Mosc)
; 76(10): 1131-9, 2011 Oct.
Article
em En
| MEDLINE
| ID: mdl-22098238
A new actinoporin Hct-S4 (molecular mass 19,414 ± 10 Da) belonging to the sphingomyelin-inhibited α-pore forming toxin (α-PFT) family was isolated from the tropical sea anemone Heteractis crispa (also called Radianthus macrodactylus) and purified by methods of protein chemistry. The N-terminal nucleotide sequence (encoding 20 amino acid residues) of actinoporin Hct-S4 was determined. Genes encoding 18 new isoforms of H. crispa actinoporins were cloned and sequenced. These genes form a multigene Hct-S family characterized by presence of N-terminal serine in the mature proteins. Highly conserved residues comprising the aromatic phosphorylcholine-binding site and significant structure-function changes in the N-terminal segment (10-27 amino acid residues) of actinoporins were established. Two expressed recombinant actinoporins (rHct-S5 and rHct-S6) were one order less hemolytically active than native actinoporins.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Anêmonas-do-Mar
/
Venenos de Cnidários
/
Citotoxinas
Limite:
Animals
Idioma:
En
Ano de publicação:
2011
Tipo de documento:
Article