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      Reviewing Chandipura: A Vesiculovirus in Human Epidemics

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          Abstract

          Chandipura virus, a member of the rhabdoviridae family and vesiculovirus genera, has recently emerged as human pathogen that is associated with a number of outbreaks in different parts of India. Although, the virus closely resembles with the prototype vesiculovirus, Vesicular Stomatitis Virus, it could be readily distinguished by its ability to infect humans. Studies on Chandipura virus while shed light into distinct stages of viral infection; it may also allow us to identify potential drug targets for antiviral therapy. In this review, we have summarized our current understanding of Chandipura virus life cycle at the molecular detail with particular interest in viral RNA metabolisms, namely transcription, replication and packaging of viral RNA into nucleocapsid structure. Contemporary research on otherwise extensively studied family member Vesicular Stomatitis Virus has also been addressed to present a more comprehensive picture of vesiculovirus life cycle. Finally, we reveal examples of protein economy in Chandipura virus life-cycle whereby each viral protein has evolved complexity to perform multiple tasks.

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          Most cited references106

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          Rapid evolution of RNA genomes.

          RNA viruses show high mutation frequencies partly because of a lack of the proofreading enzymes that assure fidelity of DNA replication. This high mutation frequency is coupled with high rates of replication reflected in rates of RNA genome evolution which can be more than a millionfold greater than the rates of the DNA chromosome evolution of their hosts. There are some disease implications for the DNA-based biosphere of this rapidly evolving RNA biosphere.
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            Identification of four conserved motifs among the RNA-dependent polymerase encoding elements.

            Four consensus sequences are conserved with the same linear arrangement in RNA-dependent DNA polymerases encoded by retroid elements and in RNA-dependent RNA polymerases encoded by plus-, minus- and double-strand RNA viruses. One of these motifs corresponds to the YGDD span previously described by Kamer and Argos (1984). These consensus sequences altogether lead to 4 strictly and 18 conservatively maintained amino acids embedded in a large domain of 120 to 210 amino acids. As judged from secondary structure predictions, each of the 4 motifs, which may cooperate to form a well-ordered domain, places one invariant amino acid in or proximal to turn structures that may be crucial for their correct positioning in a catalytic process. We suggest that this domain may constitute a prerequisite 'polymerase module' implicated in template seating and polymerase activity. At the evolutionary level, the sequence similarities, gap distribution and distances between each motif strongly suggest that the ancestral polymerase module was encoded by an individual genetic element which was most closely related to the plus-strand RNA viruses and the non-viral retroposons. This polymerase module gene may have subsequently propagated in the viral kingdom by distinct gene set recombination events leading to the wide viral variety observed today.
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              RNA-dependent RNA polymerases, viruses, and RNA silencing.

              Most viruses have RNA genomes that are replicated and transcribed into messenger RNA by viral RNA-dependent RNA polymerases (RdRps), usually in concert with other viral and host factors. Many, if not most, eukaryotes also encode putative RdRps that have been implicated in sequence-specific, RNA-triggered gene silencing. Although the viral and cellular RdRps have no sequence homology, they share functional similarities such as copying messenger RNA templates and intercellular spread of the amplified sequences. Better understanding of viral and host RdRps will improve our ability to control viruses and to use RNA silencing and viruses as tools for research, biotechnology, and medicine.
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                Author and article information

                Contributors
                +1-858-8224673 , sobasak@ucsd.edu
                +91-33-23349382 , dhrubajyotic@gmail.com
                Journal
                Biosci Rep
                Biosci. Rep
                Bioscience Reports
                Springer US (Boston )
                0144-8463
                1573-4935
                4 July 2007
                October 2007
                : 27
                : 4-5
                : 275-298
                Affiliations
                [1 ]GRID grid.266100.3, ISNI 0000000121074242, Department of Chemistry and Biochemistry, Signaling Systems Laboratory, , University of California, ; 9500 Gilman Dr, San Diego, CA 92093 USA
                [2 ]GRID grid.59056.3f, ISNI 0000000106649773, Department of Biochemistry, Dr. B. C. Guha Centre for Genetic Engineering and Biotechnology, , University of Calcutta, ; 35 B. C. Road, Kolkata, 700019 India
                Article
                9054
                10.1007/s10540-007-9054-z
                7087735
                17610154
                5a7c7568-f6bc-4a96-93e9-57dc89f8b1b5
                © The Biochemical Society 2007

                This article is made available via the PMC Open Access Subset for unrestricted research re-use and secondary analysis in any form or by any means with acknowledgement of the original source. These permissions are granted for the duration of the World Health Organization (WHO) declaration of COVID-19 as a global pandemic.

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                Original Paper
                Custom metadata
                © The Biochemical Society 2007

                Life sciences
                chandipura virus,transcription,replication,encapsidation,leader rna,nucleocapsid protein,phosphoprotein,economy,multi-functional

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