About: The SRL peptide of Rhesus Rotavirus VP4 protein governs cholangiocyte infection and the murine model of biliary atresia

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About: The SRL peptide of Rhesus Rotavirus VP4 protein governs cholangiocyte infection and the murine model of biliary atresia Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

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type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
title	The SRL peptide of Rhesus Rotavirus VP4 protein governs cholangiocyte infection and the murine model of biliary atresia
Creator	Coots, Abigail Donnelly, Bryan Dupree, Phylicia Lobeck, Inna Meller, Jaroslaw Sestak, Karol Tiao, Greg Walther, Ashley Mohanty, Sujit Mcneal, Monica
source	PMC
abstract	Biliary atresia (BA) is a neonatal obstructive cholangiopathy which progresses to end stage liver disease, often requiring transplantation. The murine model of BA, employing rhesus rotavirus (RRV), parallels human disease and has been used to elucidate mechanistic aspects of a virus induced biliary cholangiopathy. We previously reported that RRV VP4 gene plays an integral role in activating the immune system and induction of BA. Utilizing rotavirus binding and blocking assays, this study elucidated how RRV VP4 protein governs cholangiocyte susceptibility to infection both in vitro and in vivo in the murine model of BA. We identified the amino acid sequence on VP4 and its cholangiocyte binding protein, finding that the sequence is specific to those rotavirus strains which cause an obstructive cholangiopathy. Pretreatment of murine and human cholangiocytes with this VP4 derived peptide (TRTRVSRLY), significantly reduced RRV’s ability to bind and infect the cells. However, the peptide did not block cholangiocyte binding of TUCH and Ro1845, strains which do not induce murine BA. The SRL sequence within TRTRVSRLY is required for cholangiocyte binding and viral replication. The cholangiocyte membrane protein bound by SRL was found to be Hsc70. Inhibition of Hsc70 by siRNAs reduced RRV’s ability to infect cholangiocytes. This virus-cholangiocyte interaction is also seen in vivo in the murine model of BA, where inoculation of mice with TRTRVSRLY peptide significantly reduced symptoms and mortality in RRV-injected mice. CONCLUSION: The tri-peptide SRL on RRV VP4 binds to the cholangiocyte membrane protein Hsc70 defining a novel binding site governing VP4 attachment. Investigations are underway to determine the cellular response following this interaction to understand how it contributes to the pathogenesis of BA.
has issue date	2017-01-10(xsd:dateTime)
bibo:doi	10.1002/hep.28947
bibo:pmid	27859498
has license	bronze-oa
sha1sum (hex)	be876520214fb418dd059a5c06052d763dae7274
schema:url	https://doi.org/10.1002/hep.28947
resource representing a document's title	The SRL peptide of Rhesus Rotavirus VP4 protein governs cholangiocyte infection and the murine model of biliary atresia
has PubMed Central identifier	PMC5360466
has PubMed identifier	27859498
schema:publication	Hepatology
resource representing a document's body	covid:be876520214fb418dd059a5c06052d763dae7274#body_text
is schema:about of	named entity 'VP4' named entity 'induced' named entity 'rotavirus' named entity 'inoculation' named entity 'strains' named entity 'Murine' named entity 'ABBREVIATIONS' named entity 'neonatal' named entity 'induction' named entity 'virus' named entity 'strains' named entity 'biliary atresia' named entity 'vivo' named entity 'VP4' named entity 'transplantation' named entity '2017' named entity 'binding' named entity 'acid' named entity 'tripeptide' named entity 'Rotavirus' named entity 'cholangiocyte' named entity 'murine' named entity 'infection' named entity 'human disease' named entity 'binding site' named entity 'peptide' named entity 'viral replication' named entity 'cholangiocyte' named entity 'virus' named entity 'HEPATOLOGY' named entity 'rotavirus' named entity 'Hsc70' named entity 'cholangiocyte' named entity 'Biliary atresia' named entity 'binding protein' named entity 'murine' named entity 'tripeptide' named entity 'Hsc70' named entity 'pathogenesis' named entity 'virus' named entity 'Peptide' named entity 'interaction' named entity 'symptoms' named entity 'TUCH' named entity 'reovirus' named entity 'serum' named entity 'cholangiocyte' named entity 'Hsc70' named entity 'Hartford, CT' named entity 'Dharmacon' named entity 'etiology' named entity 'Cincinnati Children's Hospital Medical Center' named entity 'murine' named entity 'DAPI' named entity 'Hsc70' named entity 'blastp' named entity 'dose-dependent' named entity 'viral replication' named entity 'Hsc70' named entity 'peptide' named entity 'jaundice' named entity 'cytomegalovirus' named entity 'siRNA' named entity 'VP5' named entity 'protein' named entity 'peptide' named entity 'peptide' named entity 'Hsc70' named entity 'rotavirus' named entity 'peptide' named entity 'inoculate' named entity 'binding site'

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