Microbial production of toxins from the scorpion venom: properties and applications

Autor(es)

Amorim, Fernanda Gobbi ^[1] ; Cordeiro, Francielle Almeida ^[1] ; Pinheiro-Junior, Ernesto Lopes ^[1] ; Boldrini-Franca, Johara ^[1] ; Arantes, Eliane Candiani ^[1]

Afiliação do(s) autor(es)

^[1] Univ Sao Paulo, Sch Pharmaceut Sci Ribeirao Preto, Dept Phys & Chem, Ave Cafe S-N, BR-14040903 Ribeirao Preto, SP - Brazil

• Tipo de documento: Artigo de Revisão
• Fonte: Applied Microbiology and Biotechnology; v. 102, n. 15, p. 6319-6331, AUG 2018.
• Citações Web of Science: 1

Resumo

Scorpion venom are composed mainly of bioactive proteins and peptides that may serve as lead compounds for the design of biotechnological tools and therapeutic drugs. However, exploring the therapeutic potential of scorpion venom components is mainly impaired by the low yield of purified toxins from milked venom. Therefore, production of toxin-derived peptides and proteins by heterologous expression is the strategy of choice for research groups and pharmaceutical industry to overcome this limitation. Recombinant expression in microorganisms is often the first choice, since bacteria and yeast systems combine high level of recombinant protein expression, fast cell growth and multiplication and simple media requirement. Herein, we present a comprehensive revision, which describes the scorpion venom components that were produced in their recombinant forms using microbial systems. In addition, we highlight the pros and cons of performing the heterologous expression of these compounds, regarding the particularities of each microorganism and how these processes can affect the application of these venom components. The most used microbial system in the heterologous expression of scorpion venom components is Escherichia coli (85%), and among all the recombinant venom components produced, 69% were neurotoxins. This review may light up future researchers in the choice of the best expression system to produce scorpion venom components of interest. (AU)

• Processo FAPESP: 16/04761-4 - Caracterização estrutural, funcional e análise da resposta imune in vivo de uma serinoprotease recombinante de Crotalus durissus collilineatus modificada por PEGlação
• Beneficiário: Ernesto Lopes Pinheiro Junior
• Modalidade de apoio: Bolsas no Brasil - Doutorado Direto
• Processo FAPESP: 14/16182-3 - Novas perspectivas funcionais de uma serinoprotease de Crotalus durissus collilineatus: ação sobre canais iônicos dependentes de voltagem
• Beneficiário: Johara Boldrini França Stringari
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado
• Processo FAPESP: 11/12317-3 - Clonagem e expressão heteróloga da hialuronidase e/ou novas toxinas obtidas a partir do transcriptoma da glândula da peçonha de Tityus serrulatus
• Beneficiário: Fernanda Gobbi Amorim
• Modalidade de apoio: Bolsas no Brasil - Doutorado
• Processo FAPESP: 12/14996-8 - Clonagem e expressão de toxinas animais de interesse biotecnológico
• Beneficiário: Eliane Candiani Arantes Braga
• Modalidade de apoio: Auxílio à Pesquisa - Regular