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IN-SILICO ANALYSIS OF THE INTERACTION BETWEEN D7 PROTEIN FROM THE SALIVARY GLAND OF Ae. albopictus AND Thromboxane A2 FOR DEVELOPING ANTIPLATELET AGENT Wathon, Syubbanul; Senjarini, Kartika; Oktarianti, Rike; Lelono, Asmoro
Jurnal Bioteknologi & Biosains Indonesia (JBBI) Vol. 12 No. 1 (2025)
Publisher : BRIN - Badan Riset dan Inovasi Nasional

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.55981/jbbi.2025.8176

The salivary glands of mosquito vector diseases contain various biological components which facilitate blood-feeding into the host's body. These components are mostly protein molecules. Numerous protein molecules in the salivary glands have gained substantial research emphasis to determine their role and function, including those in the salivary glands of Ae. albopictus. D7 protein is the main component in Aedes salivary glands, which aids in inhibiting platelet aggregation by binding to the Thromboxane A2 (TxA2) during the blood-feeding. TxA2 is a eicosanoid molecule that stimulates platelet aggregation. The protein's ability to bind TxA2 shows that this protein has potential as a new antiplatelet agent. The examination of the D7 protein in binding TxA2 was performed through an in-silico approach using the molecular docking method. This research included selecting the 3D model of the D7 protein and the TxA2 ligand, preparing the 3D model of the D7 protein, native ligands, and test ligands, targeted molecular docking method, validating the molecular docking, analysis and visualization of the docking results. The molecular docking validation shows an RMSD value of 1.657 Å. The results of molecular docking show an ΔG value of -5.60 kcal/mol, meaning that the D7 protein can bind to the TxA2 ligand stably and spontaneously. The active site of the D7 protein in binding the TxA2 ligand consists of several amino acid residues, namely THR 190, GLU 268, TYR 178, PHE 154, ILE 175, ARG176, VAL 293, TYR 248, and TYR 178. The ability of D7 protein to bind TxA2 as an inducer of platelet aggregation has demonstrated its potential as a novel antiplatelet agent. These results can pave further development of drug discovery in the medical and pharmaceutical fields.

IN-SILICO ANALYSIS OF SYMBIONT BACTERIA DIVERSITY IN THE MIDGUT OF Aedes aegypti USING 16S rDNA MOLECULAR MARKERS DATABASE Wathon, Syubbanul; Finasrullah, Aufar; Oktarianti, Rike; Senjarini, Kartika
Jurnal Bioteknologi & Biosains Indonesia (JBBI) Vol. 10 No. 2 (2023)
Publisher : BRIN - Badan Riset dan Inovasi Nasional

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.55981/jbbi.2023.2841

Dengue Hemorrhagic Fever (DHF) is caused by the dengue virus, which is transmitted through Aedes aegypti mosquitoes when they feed on human blood. To effectively control the DHF vector, it is crucial to accurately characterize the symbiont bacteria associated with Ae. aegypti through an in-silico approach to identify potential targets. This study utilized in- silico analysis based on the 16S rDNA molecular marker to explore the diversity of symbiont bacteria obtained from bioinformatics databases. The analysis and visualization of bacterial diversity were conducted using the Pathosystem Resource Integration Center (PATRIC). The analysis results revealed that bacterial diversity in the midgut of Ae. aegypti, categorized as culturable and non-culturable bacteria, exhibited similar abundance patterns at the family level, albeit with varying detection rates. The most dominant taxa included the phylum Proteobacteria, class Gammaproteobacteria, order Enterobacterales, and family Enterobacteriaceae. Within the culturable bacteria category, the dominant taxa were the genus Salmonella and species Salmonella enterica, whereas the non-culturable bacteria category indicated the prevalence of the genus Escherichia and species Escherichia coli.

IN-SILICO ANALYSIS OF THE INTERACTION BETWEEN D7 PROTEIN FROM THE SALIVARY GLAND OF Ae. albopictus AND Thromboxane A2 FOR DEVELOPING ANTIPLATELET AGENT Wathon, Syubbanul; Senjarini, Kartika; Oktarianti, Rike; Lelono, Asmoro
Jurnal Bioteknologi & Biosains Indonesia (JBBI) Vol. 12 No. 1 (2025)
Publisher : BRIN - Badan Riset dan Inovasi Nasional

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.55981/jbbi.2025.8176

The salivary glands of mosquito vector diseases contain various biological components which facilitate blood-feeding into the host's body. These components are mostly protein molecules. Numerous protein molecules in the salivary glands have gained substantial research emphasis to determine their role and function, including those in the salivary glands of Ae. albopictus. D7 protein is the main component in Aedes salivary glands, which aids in inhibiting platelet aggregation by binding to the Thromboxane A2 (TxA2) during the blood-feeding. TxA2 is a eicosanoid molecule that stimulates platelet aggregation. The protein's ability to bind TxA2 shows that this protein has potential as a new antiplatelet agent. The examination of the D7 protein in binding TxA2 was performed through an in-silico approach using the molecular docking method. This research included selecting the 3D model of the D7 protein and the TxA2 ligand, preparing the 3D model of the D7 protein, native ligands, and test ligands, targeted molecular docking method, validating the molecular docking, analysis and visualization of the docking results. The molecular docking validation shows an RMSD value of 1.657 Å. The results of molecular docking show an ΔG value of -5.60 kcal/mol, meaning that the D7 protein can bind to the TxA2 ligand stably and spontaneously. The active site of the D7 protein in binding the TxA2 ligand consists of several amino acid residues, namely THR 190, GLU 268, TYR 178, PHE 154, ILE 175, ARG176, VAL 293, TYR 248, and TYR 178. The ability of D7 protein to bind TxA2 as an inducer of platelet aggregation has demonstrated its potential as a novel antiplatelet agent. These results can pave further development of drug discovery in the medical and pharmaceutical fields.

PURIFIKASI FRAKSI PROTEIN IMUNOGENIK 47 kDa DARI KELENJAR SALIVA Aedes albopictus SEBAGAI TARGET PENGEMBANGAN VAKSIN DENGUE BERBASIS VEKTOR Wathon, Syubbanul; Rahmawati, Itsna; Oktarianti, Rike; Lelono, Asmoro; Senjarini, Kartika
Berita Biologi Vol 22 No 1 (2023): Berita Biologi
Publisher : BRIN Publishing (Penerbit BRIN)

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.55981/beritabiologi.2023.810

Kapasitas vektorial Ae. albopictus telah diketahui sebagai vektor potensial virus dengue yang mengakibatkan DBD. Transmisi virus dengue terjadi ketika Ae. albopictus melakukan blood feeding ke manusia yang difasilitasi oleh aktivitas biologis protein pada kelenjar saliva vektor. Penelitian kami sebelumnya menunjukkan fraksi protein 47 kDa dari kelenjar saliva Ae. albopictus bersifat imunogenik. Protein 47 kDa merupakan serpins family yang diduga sebagai antikoagulan dan berperan sebagai protease inhibitor sehingga mempermudah transmisi virus dengue. Peran protein tersebut mengindikasikan adanya potensi dalam pengembangan vaksin penghambat transmisi patogen melalui vaksinasi melawan protein tersebut sehingga dapat menghambat transmisi dengue. Studi potensi protein tersebut memerlukan ekstrak murni, maka purifikasi protein target merupakan langkah yang sangat penting. Penelitian ini dimulai dengan landing collection dan rearing Ae. albopictus, isolasi dan ekstraksi protein kelenjar saliva, isolasi fraksi protein 47 kDa melalui SDS-PAGE, purifikasi protein, analisis dot blot dan western blot. Analisis SDS-PAGE menunjukkan pita tunggal protein target 47 kDa dari kelenjar saliva Ae. albopictus yang berhasil dipurifikasi menggunakan Electroeluter. Analisis dot blot menunjukkan protein 47 kDa terdeteksi bersifat imunogenik dan dikonfirmasi melalui analisis western blot bahwa protein target hasil purifikasi memiliki berat molekul 47 kDa.

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