Tentacles of venom: toxic protein convergence in the Kingdom Animalia.
J Mol Evol
; 68(4): 311-21, 2009 Apr.
Article
em En
| MEDLINE
| ID: mdl-19294452
ABSTRACT
The origin and evolution of venom in many animal orders remain controversial or almost entirely uninvestigated. Here we use cDNA studies of cephalopod posterior and anterior glands to reveal a single early origin of the associated secreted proteins. Protein types recovered were CAP (CRISP, Antigen 5 [Ag5] and Pathogenesis-related [PR-1]), chitinase, peptidase S1, PLA(2) (phospholipase A(2)), and six novel peptide types. CAP, chitinase, and PLA(2) were each recovered from a single species (Hapalochlaena maculosa, Octopus kaurna, and Sepia latimanus, respectively), while peptidase S1 transcripts were found in large numbers in all three posterior gland libraries. In addition, peptidase S1 transcripts were recovered from the anterior gland of H. maculata. We compare their molecular evolution to that of related proteins found in invertebrate and vertebrate venoms, revealing striking similarities in the types of proteins selected for toxic mutation and thus shedding light on what makes a protein amenable for use as a toxin.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peçonhas
/
Evolução Molecular
/
Cefalópodes
/
Venenos de Moluscos
Limite:
Animals
Idioma:
En
Revista:
J Mol Evol
Ano de publicação:
2009
Tipo de documento:
Article
País de afiliação:
Austrália
País de publicação:
ALEMANHA
/
ALEMANIA
/
DE
/
DEUSTCHLAND
/
GERMANY