Investigation of the ability of the oviposition-stimulant lectin from Moringa oleifera seeds (WSMoL) to bind with membrane proteins present in the legs of Aedes aegypti

• Published in: International journal of biological macromolecules Vol. 162; pp. 657 - 662
• Main Authors: Silva, Livia Lais de Santana, Santos, Nataly Diniz de Lima, Silva, Stella Cristina Cabral, Lima, Thâmarah de Albuquerque, Coelho, Luana Cassandra Breitenbach Barroso, Zingali, Russolina Benedeta, Navarro, Daniela Maria do Amaral Ferraz, Napoleão, Thiago Henrique, Paiva, Patrícia Maria Guedes
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01-11-2020
• Subjects: ABC carriers; Aedes - anatomy & histology; Aedes - chemistry; Affinity chromatography; Animals; Insect Proteins - chemistry; Insect Proteins - metabolism; Insecticide lectin; Membrane Proteins - chemistry; Membrane Proteins - metabolism; Moringa oleifera - chemistry; Oviposition - drug effects; Oviposition behavior; Plant Lectins - chemistry; Plant Lectins - pharmacology; Yellow fever mosquito; ABC carriers; Yellow fever mosquito; Affinity chromatography; Insecticide lectin; Oviposition behavior
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2020.06.189

The mosquito Aedes aegypti L. is a vector transmitting diseases such as dengue, chikungunya and Zika virus fever. The water-soluble lectin from Moringa oleifera Lam. seeds (WSMoL) is larvicidal, ovicidal and can stimulate oviposition in A. aegypti. This study aimed to investigate whether WSMoL could bind to membrane proteins from A. aegypti legs. Initially, proteins from the legs were extracted using sodium deoxycholate, digitonin, dodecyl sodium sulfate (SDS) or Triton X-100. The protein concentration was found to be higher in the extract obtained using Triton X-100, which was applied to a WSMoL-Sepharose column. The adsorbed proteins were evaluated using gel filtration chromatography and polyacrylamide gel electrophoresis (PAGE) in presence of SDS. The similarity in the sequences of adsorbed proteins with those available in databases was determined. The proteins adsorbed on the matrix were eluted forming a single peak. Gel filtration chromatography and SDS-PAGE revealed the presence of proteins with molecular masses of approximately 20 kDa and polypeptide bands of 17.0 and 23.7 kDa, respectively. MS/MS analysis indicated similarity between these proteins and ABC carriers, which are expressed in the legs of mosquitos. WSMoL could bind to membrane proteins in the legs of A. aegypti females and induce oviposition through these interactions.