Abstract
Nipah virus (NiV) is an emerging and priority pathogen from the Paramyxoviridae family with a high fatality rate. It causes various diseases such as respiratory ailments and encephalitis and poses a great threat to humans and livestock. Despite various efforts, there is no approved antiviral treatment available. Therefore, to expedite and assist the research, we have developed an integrative resource NipahVR (http://bioinfo.imtech.res.in/manojk/nipahvr/) for the multi-targeted putative therapeutics and epitopes for NiV. It is structured into different sections, i.e. genomes, codon usage, phylogenomics, molecular diagnostic primers, therapeutics (siRNAs, sgRNAs, miRNAs) and vaccine epitopes (B-cell, CTL, MHC-I and -II binders). Most decisively, potentially efficient therapeutic regimens targeting different NiV proteins and genes were anticipated and projected. We hope this computational resource would be helpful in developing combating strategies against this deadly pathogen.Database URL: http://bioinfo.imtech.res.in/manojk/nipahvr/
Highlights
Nipah virus (NiV) is a highly pathogenic virus closely related to the Hendra virus (HeV) from the genus Henipavirus of the family Paramyxoviridae
V and W proteins are produced by RNA editing and localized in the cytoplasm and nucleus, respectively, and the second open reading frame (ORF) generates C protein
Very few computational studies focusing on the NiV are performed, and there is no such kind of therapeutic web resource available for it
Summary
Nipah virus (NiV) is a highly pathogenic virus closely related to the Hendra virus (HeV) from the genus Henipavirus of the family Paramyxoviridae. NiV is an enveloped single-stranded RNA (ssRNA), a negative-sense virus of size ∼18 250 nucleotides It encodes nine proteins namely nucleoprotein (N), four proteins encoded by P gene (phosphoprotein (P), W, V, C protein), matrix (M) protein, fusion (F) glycoprotein, attachment glycoproteins (G) and a large polymerase (L) protein [1,2,3]. Viral G protein (attachment protein) first binds to the Ephrin-B2 or B3 cellular receptors found on the neuron, smooth muscles, capillaries and. The largest NiV protein L retains all the enzymatic functions like genome replication and transcription for the viral RNA synthesis [1,2,3]
Sign-in/Register to view highlights & summary Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Database : the journal of biological databases and curation
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
