Article

Dengue fever and dengue hemorrhagic fever: a review of the history, transmission, treatment, and prevention.

Baylor College of Medicine, Department of Pediatrics, Houston, Texas 77030, USA.
Seminars in Pediatric Infections Diseases 02/2005; 16(1):60-5. DOI: 10.1053/j.spid.2004.09.013
Source: PubMed
0 Followers
 · 
122 Views
  • [Show abstract] [Hide abstract]
    ABSTRACT: Non Structural protein 3 (NS3) constitute protease, helicase and polymerase that are essential for dengue virus replication. The aim of the present study is to block the replication of the virus by targeting the NS3 Protein. The retrieved sequences of NS3 protein from National Centre for Biotechnology information (NCBI) shows that the antigenic sites of the protein are highly variable in all the four serotypes of dengue virus (DENV) i.e. DENV I, DENV II, DENV III and DENV IV. DENV III found to be most distantly related serotype among all the serotypes studied using UPGMA method. The 3D structure of NS3 protein was modeled using homology modeling by MODELLER 9v8. Evaluation of the constructed NS3 protein models were done by PROCHECK, WhatIf using Exome Horizon. The derived compounds of mycophenolic acid and ribavirin were docked as ligands to the constructed models of NS3 protein using Autodock 4.2 for Protein-ligand interaction study
    Bangladesh Journal of Pharmacology 02/2014; 9(1):83-95. DOI:10.3329/bjp.v9i1.17583 · 0.51 Impact Factor
  • Source
    [Show abstract] [Hide abstract]
    ABSTRACT: The aim of this study was to evaluate the larvicidal activity of Mentha x villosa essential oil (MVEO) and its major constituent, rotundifolone, against larvae of Aedes aegypti. Additionally, a set of 15 analogues of the rotundifolone were evaluated to identify the molecular characteristics which contribute to the larvicidal effect. The results from the present study showed that the MVEO exhibited outstanding toxic effects against Ae. aegypti larvae (LC50=45.0ppm). Rotundifolone exhibited reasonable larvicidal activity (LC50=62.5ppm). With respect to comparative study of rotundifolone and its analogues, all tested compounds were less potent than rotundifolone, except (-)-limonene. In general, replacement of C-C double bonds by epoxides groups decreases the larvicidal potency. The presence of α,β-unsaturated carbonyls contributes to the larvicidal toxicity. The addition of hydroxyl groups in the chemical structure resulted in less potent compounds. Furthermore, the enantioselectivity seems to play an important role for the larvicidal toxicity.
    Chemosphere 11/2013; 104. DOI:10.1016/j.chemosphere.2013.10.035 · 3.50 Impact Factor
  • [Show abstract] [Hide abstract]
    ABSTRACT: Bacillus thuringiensis subsp. israelensis (Bti) has been widely for the biological control of mosquito populations. However, the mechanism of Bti toxins is still not fully understood. To further elucidate the mechanism of Bti toxins, we developed an Aedes aegypti resistant strain that shows high-level resistance to Cry11Aa toxin. After 27 selections with Cry11Aa toxin, the larvae showed a 124-fold resistance ratio for Cry11Aa (strain G30). G30 larvae showed cross-resistance to Cry4Aa (66-fold resistance), less to Cry4Ba (13-fold), but not to Cry11Ba (2-fold). Midguts from these resistant larvae did not show detectable difference in the processing of the Cry11Aa toxin compared to that in susceptible larvae (WT). Brush border membrane vesicles (BBMV) from resistant larvae bound slightly less Cry11Aa compared to WT BBMV. To identify potential proteins associated with Cry11A resistance, not only transcript changes in the larval midgut were analyzed using Illumina sequencing and qPCR, but alterations of previously identified receptor proteins were investigated using immunoblots. The transcripts of 375 genes were significantly increased and those of 208 genes were down regulated in the resistant larvae midgut compared to the WT. None of the transcripts for previously identified receptors of Cry11Aa (Aedes cadherin, ALP1, APN1, and APN2) were altered in these analyses. The genes for the identified functional receptors in resistant larvae midgut did not contain any mutation in their sequences nor was there any change in their transcript expression levels compared to WT. However, ALP proteins were expressed at reduced levels (∼40%) in the resistant strain BBMV. APN proteins and their activity were also slightly reduced in resistance strain. The transcript levels of ALPs (AAEL013330 and AAEL015070) and APNs (AAEL008158, AAEL008162) were significantly reduced. These results strongly suggest that ALPs and APNs could be associated with Cry11Aa resistance in Ae. aegypti.
    Insect Biochemistry and Molecular Biology 09/2014; 54. DOI:10.1016/j.ibmb.2014.09.004 · 3.42 Impact Factor