Bacterial chromosomes often carry integrated genetic elements (e.g., plasmids, transposons, prophages, and islands) whose precise function and contribution to the evolutionary fitness of the host bacterium are unknown. The CTXϕ prophage, which encodes cholera toxin in Vibrio cholerae1, is known to be adjacent to a chromosomally integrated element of unknown function termed the toxin-linked cryptic (TLC)2. Here we report characterization of a TLC-related element that corresponds to the genome of a satellite filamentous phage (TLC-Knϕ1) which uses the morphogenesis genes of another filamentous phage (fs2ϕ) to form infectious TLC-Knϕ1 phage particles. The TLC-Knϕ1 phage genome carries a sequence similar to the dif recombination sequence which functions in chromosome dimer resolution using XerC and XerD recombinases3. The dif sequence is also exploited by lysogenic filamentous phages (e.g., CTXϕ) for chromosomal integration of their genomes. Bacterial cells defective in the dimer resolution often show an aberrant filamentous cell morphology3,4. We found that acquisition and chromosomal integration of the TLC-Knϕ1 genome restored a perfect dif site and normal morphology to V. cholerae wild type and mutant strains that displayed dif -filamentation phenotypes. Furthermore, lysogeny of a dif -nontoxigenic V. cholerae with TLC-Knϕ1 promoted its subsequent toxigenic conversion through integration of CTXϕ into the restored dif site. These results reveal a remarkable level of cooperative interactions between multiple filamentous phages in the emergence of the bacterial pathogen that causes cholera.The TLC element of V. cholerae encodes the Cri replicase with homology to filamentous phage replication proteins and TlcR, a protein that displays sequence similarity to RstR, the Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms * Corresponding author: Mailing address: Shah M. Faruque, Molecular Genetics Laboratory, International Centre for Diarrhoeal Disease Research, Bangladesh, Dhaka-1212, Bangladesh., Phone: (+880 2) 8860523 through 8860532, Fax : (+880 2) 8812529, faruque@icddrb.org. Author contributions. F.H., M.K., and S.M.F. conducted the experiments, and performed analyses of bacterial strains and phages. S.M.F. and J.J.M. designed the studies, analyzed data and wrote the manuscript. Relevant nucleotide sequence data described in the article have been deposited at GenBank under accession numbers HM134797, HM134798, HM134799, and HM134800.Supplementary Information is linked to the online version of the paper at www.nature.com/nature. repressor controlling lysogeny of the filamentous CTXϕ and the target for anti-repression by the RstC product of satellite filamentous phage RS1ϕ1,2,5-9. For these reasons we hypothesized that the TLC element corresponds to the genome of a satellite filamentous phage that depended on another fi...
Nipah virus (NiV) is highly pathogenic single-stranded negative sense RNA virus. It can cause severe encephalitis and respiratory disease in humans. In addition, NiV infects a large range of host including mammals. As a result of its higher zoonotic potential and pathogenicity for human, it has been rated as an alert in recent days. A therapeutic treatment or vaccines has become elusive to fight against this virus. In this study, the attachment (G) and fusion (F) glycoproteins of NiV, responsible for the viral attachment and entry to the host cell, were selected to develop epitope-based vaccine against Nipah virus. Epitopes were identified from the conserved region of G and F protein of NiV. Both B-cell and T-cell immunity were checked to affirm it that these epitopes will be able to induce humoral and cellular immunity. A total of 6 T-cell epitopes and 19 significant HLA-epitope interactions were identified. Eventually it has shown an acceptable percentage in population coverage (46.45 %) and efficient binding with HLA molecule by molecular docking study.
BackgroundLarge scale understanding of complex and dynamic alterations in cellular and subcellular levels during cancer in contrast to normal condition has facilitated the emergence of sophisticated systemic approaches like network biology in recent times. As most biological networks show modular properties, the analysis of differential modularity between normal and cancer protein interaction networks can be a good way to understand cancer more significantly. Two aspects of biological network modularity e.g. detection of molecular complexes (potential modules or clusters) and identification of crucial nodes forming the overlapping modules have been considered in this regard.MethodsIn the current study, the computational analysis of previously published protein interaction networks (PINs) has been conducted to identify the molecular complexes and crucial nodes of the networks. Protein molecules involved in ten major cancer signal transduction pathways were used to construct the networks based on expression data of five tissues e.g. bone, breast, colon, kidney and liver in both normal and cancer conditions. MCODE (molecular complex detection) and ModuLand methods have been used to identify the molecular complexes and crucial nodes of the networks respectively.ResultsIn case of all tissues, cancer PINs show higher level of clustering (formation of molecular complexes) than the normal ones. In contrast, lower level modular overlapping is found in cancer PINs than the normal ones. Thus a proposition can be made regarding the formation of some giant nodes in the cancer networks with very high degree and resulting in reduced overlapping among the network modules though the predicted molecular complex numbers are higher in cancer conditions.ConclusionThe study predicts some major molecular complexes that might act as the important regulators in cancer progression. The crucial nodes identified in this study can be potential drug targets to combat cancer.
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