Palavras-chave
Alvos proteicos
Desenvolvimento de inseticidas
Alvos moleculares
Como Citar
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Resumo
Objetivo: Identificar as principais proteínas de Aedes aegypti investigadas no desenvolvimento de inseticidas. Métodos: Foi realizada uma revisão da literatura científica publicada entre 2014 e 2024 utilizando as bases de dados Pubmed, ScienceDirect e Scopus, com os descritores "Aedes aegypti", "proteínas-alvo" e "modo de ação". Foram incluídos artigos experimentais revisados por pares e publicados em inglês. Os estudos selecionados foram analisados de acordo com os tipos de proteínas-alvo investigadas e as abordagens metodológicas utilizadas (in silico, in vitro e in vivo). Resultados: Dos 335 artigos inicialmente recuperados, 17 atenderam aos critérios de inclusão. A glutationa S-transferase (GST) foi o alvo de detoxificação mais frequentemente investigado, seguida por diversas isoformas de GST. Os principais alvos metabólicos incluíram a proteína de ligação ao odor 1 (OBP1), a 3-hidroxiquinurenina transaminase (HKT), a acetilcolinesterase (AChE), a proteína transportadora de esteróis 2 (SCP-2) e a anidrase carbônica (CA). Os alvos relacionados à neurotransmissão compreenderam o receptor dopaminérgico AaDOP2 e os cotransportadores de cloreto-cátion CCC2 e CCC3. Conclusão: Os resultados destacam os alvos proteicos como uma estratégia promissora para o controle de A. aegypti e enfatizam a necessidade de identificar novos alvos moleculares para inseticidas mais eficazes e sustentáveis.
Referências
AGUIAR GRF, et al. Common arboviruses and the kidney: a review. Brazilian Journal of Nephrology, 2024; 46(3), 1-11.
ALBUQUERQUE BNL, et al. Oviposition deterrence, larvicidal activity and docking of β-germacrene-D-4-ol obtained from leaves of Piper corcovadensis (Piperaceae) against Aedes aegypti. Industrial Crops and Products, 2022; 182: 1-11.
ARAÚJO MO, et al. Larvicidal activity of cinnamic acid derivatives: investigating alternative products for Aedes aegypti L. control. Molecules, 2020; 26(1): 1-21.
BEYENBACH KW, et al. Targeting renal epithelial channels for the control of insect vectors. Tissue Barriers, 2015; 3(1): 1-14.
BEZERRA WAS, et al. In vitro and in silico evaluation of plant compounds as inhibitors of glutathione S-transferase from Rhipicephalus microplus and R. decoloratus. Molecular and Biochemical Parasitology, 2026; 1-7.
CONLEY JM, et al. Evaluation of AaDOP2 receptor antagonists reveals antidepressants and antipsychotics as novel lead molecules for control of the yellow fever mosquito, Aedes aegypti. The Journal of Pharmacology and Experimental Therapeutics, 2015; 352(1): 53-60.
DONG S, et al. Pleiotropic Odorant-Binding Proteins Promote Aedes aegypti Reproduction and Flavivirus Transmission. mBio, 2021; 12(5): 1-18.
EBIHARA K, and NIWA, R. Compounds inhibiting noppera-bo, a glutathione S-transferase involved in insect ecdysteroid biosynthesis: novel insect growth regulators. Biomolecules, 2023; 13(3): 1-12.
FARIA-REIS A, et al. Silencing of the 20S proteasomal subunit-α6 triggers full oogenesis arrest and increased mRNA levels of the selective autophagy adaptor protein p62/SQSTM1 in the ovary of the vector Rhodnius prolixus. PLOS Neglected Tropical Diseases, 2023; 17(6): 1-23.
HIBINO H, et al. Inwardly rectifying potassium channels: their structure, function, and physiological roles. Physiological Reviews, 2010; 90(1): 1-76.
JOHNSON EJ, et al. Bioinsecticidal activity of cajeput oil to pyrethroid-susceptible and-resistant mosquitoes. Pesticide Biochemistry and Physiology, 2023; 193:1-10.
KOK BH, et al. Dengue virus infection–a review of pathogenesis, vaccines, diagnosis and therapy. Virus research, 2023; 324: 11-17.
KOSTAROPOULOS I, et al. Glutathione S-transferase in the defence against pyrethroids in insects. Insect Biochem Mol Biol. 2001; 31(4-5): 1-7.
LIMA-CÂMARA TN, et al. Arboviroses emergentes e desafios de saúde pública no Brasil. Revista Saúde Púlica, 2016; 50: 1-7.
MACIEL LG, et al. Discovery of 1, 2, 4-oxadiazole derivatives as a novel class of noncompetitive inhibitors of 3-hydroxykynurenine transaminase (HKT) from Aedes aegypti. Bioorganic & Medicinal Chemistry, 2020; 28(2): 1-20.
MACIEL LG, et al. A second generation of 1,2,4-oxadiazole derivatives with enhanced solubility for inhibition of 3-hydroxykynurenine transaminase (HKT) from Aedes aegypti. RSC Medicinal Chemistry, 2021; 12(2): 1-15.
MACIEL LG, et al. Inhibition of 3-Hydroxykynurenine Transaminase from Aedes aegypti and Anopheles gambiae: a mosquito-specific target to combat the transmission of arboviruses. ACS Bio & Med Chem Au, 2023; 3(2):1-12.
MANNERVIK B. Glutathione transferases structure and catalytic activity. CRC Crit. Rev. Biochem, 1976;23(281-334): 1-55.
MEYER JM, et al. A “Genome-to-Lead” Approach for Insecticide Discovery: Pharmacological Characterization and Screening of Aedes aegypti D(1)-like Dopamine Receptors. PLoS Neglected Tropical Diseases, 2012; 6(1):1-15.
MOURÃO EDS, et al. Identification of molecular scaffolds from Caatinga Brazilian biome with potential against Aedes aegypti by molecular docking and molecular dynamics simulations. Journal of Molecular Structure, 2021; 1229: 1-7.
MUTUNGA JM. et al. Mosquito acetylcholinesterase as a target for novel phenyl-substituted carbamates. International Journal of Environmental Research and Public Health, 2019; 16(9): 1-13.
OLIVEIRA JHM, et al. Blood-feeding triggers heme-induced oxidative stress and differential expression of GSTs in Aedes aegypti. Frontiers in Physiology, 2020;4(11): 1-11.
PELOSI P, et al. Beyond chemoreception: diverse tasks of soluble olfactory proteins in insects. Biological Reviews, Cambridge, 2018; 93(1): 1-17.
PIERMARINI PM, et al. Localization and role of inward rectifier potassium channels in Malpighian tubules of the yellow fever mosquito Aedes aegypti. Insect Biochemistry and Molecular Biology, 2015; 66: 1–15.
PIERMARINI PM, et al. Malpighian Tubules as Novel Targets for Mosquito Control. International Journal of Environmental Research and Public Health, 2017; 14(2): 1-15.
POURZANGIABADI M. et al. Dengue virus: Etiology, epidemiology, pathobiology, and developments in diagnosis and control – A comprehensive review. Infection, Genetics and Evolution, 2024; 127: 1-14.
RANA A, et al. Insight into insect odorant binding proteins: an alternative approach for pest management. Journal of Natural Pesticide Research, 2024; 8: 1-11.
RANSON H, et al. The role of alternative mRNA splicing in generating heterogeneity within the Anopheles gambiae class I glutathione S-transferase family. Proceedings of the National Academy of Sciences, 1998;95(24): 1-6.
RAPHEMOT R, et al. Eliciting renal failure in mosquitoes with a small-molecule inhibitor of inward-rectifying potassium channels. PloS ONE, 2013; 8(5): 1-7.
ROUHIER MF, et al. Pharmacological validation of an inward-rectifier potassium (Kir) channel as an insecticide target in the yellow fever mosquito Aedes aegypti. PloS One, 2014; 9(6): 1-7.
SANTOS ELVS, et al. Essential Oil of Ocimum basilicum against Aedes aegypti and Culex quinquefasciatus: Larvicidal activity of a nanoemulsion and in silico study. Separations, 2024; 11(4): 1-21.
SANTOS LLM et al. Dengue, chikungunya, and Zika virus infections in Latin America and the Caribbean: a systematic review. Revista panamericana de salud publica, 2023; 47: 1-9.
SETLUR AS, et al. Comprehensive molecular interaction studies to construe the repellent/kill activity of geraniol during binding event against Aedes aegypti proteins. Molecular Biotechnology, 2022; 65(5): 726-740.
SHAHID M, et al. Synthesis, DFT study, molecular docking and larvicidal activity of Chitin inhibitor alanine derived compounds. Polyhedron, 2023; 245: 1-4.
SILVA AS, et al. Larvicidal activity and docking study of Ramalina complanata and Cladonia verticillaris extracts and secondary metabolites against Aedes aegypti. Industrial Crops and Products, 2023; 195: 1-8.
SPADAR A, et al. Uncovering the genetic diversity in Aedes aegypti insecticide resistance genes through global comparative genomics. Scientific Reports, 2024; 14(1): 1-12.
SUSSMAN JL, et al. Atomic structure of acetylcholinesterase from Torpedo californica: a prototypic acetylcholine-binding protein. Science, 1991; 253(5022): 1-8.
SWALE DR, et al. An insecticide resistance-breaking mosquitocide targeting inward rectifier potassium channels in vectors of Zika virus and malaria. Scientific Reports, 2016; 6(1): 1-11.
WANG J, et al. Aedes aegypti Odorant Binding Protein 22 selectively binds fatty acids through a conformational change in its C-terminal tail. Scientific Reports, 2020. 1-15.
WORLD HEALTH ORGANIZATION (WHO). Dengue – the Region of the Americas. Situation Report, 14
December 2023. Disponível em PAHO/WHO on-line. Acesso em: 29 de julho de 2025.