To control malaria, researchers are focused on immunogenic protein to develop a vaccine against this life-threatening disease. The target immunogenic proteins against parasite infection and other diseases are mostly focused on GPI-anchor proteins. AgSGU is secretory glycoconjugate, the second most expressed protein in mosquito midgut after blood feeding. Recent studies confirmed that Pfs47 is the key protein for ookinetes invasion in the mosquito midgut and AGAP006398 act as a receptor for Pfs47. Protein interaction pathway analysis using bioinformatics approaches shows that AgSGU makes a complex with AGAP006398 and Pfs47, so here we target AgSGU protein for its functional and molecular characterization. Blastp analysis showing its conservancy in most Anopheles mosquito species. Phylogenetic evolutionary analysis shows that AgSGU is an independently evolved protein and closely related to ACON000570 in Anopheles coluzzii. Domain architecture analysis results that it is composed of a single MBF2 domain which acts as a transcriptional activator factor. The 3-D structure was prepared by I-TASSER and refined with the Galaxy Refine tool. The calculated RMSD value for the predicted structure was 0.558, suggesting the reliability of the 3-D structure. AgSGU was docked with AGAP006398 and Pfs47 and interacted effectively with both the protein. The antigenicity evaluation confirmed its potential to activate the immune response. The C-ImmSim immune response analysis proved that AgSGU protein activates both humoral and acquired immune responses. Finally, these studies conclude that AgSGU protein is a potential target for developing a transmission-blocking vaccine against malaria.
The insecticidal resistance of mosquitoes necessitates the development of a natural, safe, and plant-based method for vector control. Unfortunately, there are no effective vaccines or particular medications available to combat malaria; therefore, mosquitoes must be targeted directly. Previous studies have shown the health benefits of Datura stramonium, but its bioactive peptides or proteins are less explored. This is the first study on D. stramonium stem protein used for mosquito larval protein. The present study aimed to identify the purified mosquito larval protein from the crude extract of D. stramonium stem. Crude protein was isolated, precipitated, dialyzed, and purified by using ion-exchange chromatography, native PAGE, and HPLC. The highest larval mortality was observed at 5.5 mg/ml of crude protein concentration. Native PAGE was used for the analysis and purification of active proteins. The single homogeneous purified larvicidal protein appeared as a single band of 30 kDa by SDS-PAGE. The novel bioactive peptide was characterized by LC-MS/ESI-MS. The homology of the peptide was searched by the Mascot search engine. The database search revealed has not shown peptide similarity with D. stramonium protein, but homology with another plant Arabidopsis thaliana protein is probable for protein phosphatases. The lethal concentration of purified protein against 3rd instar larvae of Anopheles stephensi had LC50 and LC90 values of 25 μg/ml and 40 μg/ml. It has shown new insight into larvicidal activity and can be used as a new drug against malaria and other mosquito-borne diseases.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.