Peptides of arachnid venoms with insecticidal activity targeting sodium channels.
Arachnids have a venom apparatus and secrete a complex chemical mixture of low molecular mass organic molecules, enzymes and polypeptide neurotoxins designed to paralyze or kill their prey. Most of these toxins are specific for membrane voltage-gated sodium channels, although some may also target calcium or potassium channels and other membrane receptors. Scorpions and spiders have provided the greatest number of the neurotoxins studied so far, for which, a good number of primary and 3D structures have been obtained. Structural features, comprising a folding that determines a similar spatial distribution of charged and hydrophobic side chains of specific amino acids, are strikingly common among the toxins from spider and scorpion venoms. Such similarities are, in turn, the key feature to target and bind these proteins to ionic channels. The search for new insecticidal compounds, as well as the study of their modes of action, constitutes a current approach to rationally design novel insecticides. This goal tends to be more relevant if the resistance to the conventional chemical products is considered. A promising alternative seems to be the biotechnological approach using toxin-expressing recombinant baculovirus. Spider and scorpion toxins having insecticidal activity are reviewed here considering their structures, toxicities and action mechanisms in sodium channels of excitable membranes.
De Lima
M E
ME
Lab. Venenos e Toxinas Animais, Universidade Federal de Minas Gerais, 31.270-901, Belo Horizonte, MG, Brasil; Núcleo de Biomoléculas - Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, 31.270-901, Belo Horizonte, MG, Brasil. Electronic address: delima@icb.ufmg.br.
Figueiredo
S G
SG
Centro de Ciências Fisiológicas, CBM - Universidade Federal do Espírito Santo, Vitória, ES, Brasil.
Pimenta
A M C
AMC
Lab. Venenos e Toxinas Animais, Universidade Federal de Minas Gerais, 31.270-901, Belo Horizonte, MG, Brasil; Núcleo de Biomoléculas - Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, 31.270-901, Belo Horizonte, MG, Brasil.
Santos
D M
DM
Lab. Venenos e Toxinas Animais, Universidade Federal de Minas Gerais, 31.270-901, Belo Horizonte, MG, Brasil; Núcleo de Biomoléculas - Instituto de Ciências Biológicas, Universidade Federal de Minas Gerais, 31.270-901, Belo Horizonte, MG, Brasil.
Borges
M H
MH
Lab. Venenos e Toxinas Animais, Universidade Federal de Minas Gerais, 31.270-901, Belo Horizonte, MG, Brasil; Centro de Pesquisa Prof. Carlos R. Diniz, Fundação Ezequiel Dias, Belo Horizonte, MG, Brasil.
Cordeiro
M N
MN
Centro de Pesquisa Prof. Carlos R. Diniz, Fundação Ezequiel Dias, Belo Horizonte, MG, Brasil.
Richardson
M
M
Centro de Pesquisa Prof. Carlos R. Diniz, Fundação Ezequiel Dias, Belo Horizonte, MG, Brasil.
Oliveira
L C
LC
Departamento de Farmácia Bioquímica - Universidade Federal dos Vales do Jequitinhonha e Mucuri, 39100-000, Diamantina, MG, Brasil.
Stankiewicz
M
M
Laboratory of Biophysics - Institute of General and Molecular Biology, N. Copernicus University, 87-100, Torun, Poland.
Pelhate
M
M
Lab. Récepteurs et Canaux Ioniques Membranaires, Université d'Angers, 49045, Angers, France.
D000818:Animals; D001097:Arachnida / Q000502:physiology*; D001369:Axons / Q000187:drug effects / Q000502:physiology; D019476:Insect Proteins / Q000737:chemistry / Q000633:toxicity*; D007473:Ion Channels / Q000037:antagonists & inhibitors / Q000187:drug effects* / Q000378:metabolism; D009498:Neurotoxins / Q000737:chemistry / Q000633:toxicity*; D010455:Peptides / Q000737:chemistry / Q000633:toxicity*; D010572:Pest Control, Biological; D017510:Protein Folding; D012605:Scorpions / Q000502:physiology; D013111:Spider Venoms / Q000737:chemistry / Q000633:toxicity*; D013112:Spiders / Q000502:physiology
D019476:Insect Proteins; D007473:Ion Channels; D009498:Neurotoxins; D010455:Peptides; D013111:Spider Venoms