Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/12432
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dc.contributor.authorSomrit M.
dc.contributor.authorYu S.-Y.
dc.contributor.authorLe Pendu J.
dc.contributor.authorBreiman A.
dc.contributor.authorGuérardel Y.
dc.contributor.authorWeerachatyanukul W.
dc.contributor.authorWatthammawut A.
dc.date.accessioned2021-04-05T03:03:22Z-
dc.date.available2021-04-05T03:03:22Z-
dc.date.issued2020
dc.identifier.issn14625814
dc.identifier.other2-s2.0-85090950583
dc.identifier.urihttps://ir.swu.ac.th/jspui/handle/123456789/12432-
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85090950583&doi=10.1111%2fcmi.13258&partnerID=40&md5=6ed4b7fc0937abca60c9f40d3a25124f
dc.description.abstractThe Macrobrachium rosenbergii nodavirus (MrNV), the causative agent of white-tail disease (WTD) in many species of shrimp and prawn, has been shown to infect hemocytes and tissues such as the gills and muscles. However, little is known about the host surface molecules to which MrNV attach to initiate infection. Therefore, the present study investigated the role of glycans as binding molecules for virus attachment in susceptible tissues such as the gills. We established that MrNV in their virus-like particle (MrNV-VLP) form exhibited strong binding to gill tissues and lysates, which was highly reduced by the glycan-reducing periodate and PNGase F. The broad, fucose-binding Aleuria Aurantia lectin (AAL) highly reduced MrNV-VLPs binding to gill tissue sections and lysates, and efficiently disrupted the specific interactions between the VLPs and gill glycoproteins. Furthermore, mass spectroscopy revealed the existence of unique fucosylated LacdiNAc-extended N-linked and O-linked glycans in the gill tissues, whereas beta-elimination experiments showed that MrNV-VLPs demonstrated a binding preference for N-glycans. Therefore, the results from this study highly suggested that MrNV-VLPs preferentially attach to fucosylated N-glycans in the susceptible gill tissues, and these findings could lead to the development of strategies that target virus-host surface glycan interactions to reduce MrNV infections. © 2020 John Wiley & Sons Ltd
dc.rightsSrinakharinwirot University
dc.subjectfucose
dc.subjectglycan
dc.subjectglycoprotein
dc.subjectlectin
dc.subjectperiodate
dc.subjectAleuria aurantia
dc.subjectanimal cell
dc.subjectanimal tissue
dc.subjectArticle
dc.subjectbinding site
dc.subjectcell lysate
dc.subjectcontrolled study
dc.subjectfreshwater species
dc.subjectfucosylation
dc.subjectgill
dc.subjectMacrobrachium rosenbergii
dc.subjectmass spectrometry
dc.subjectNodaviridae
dc.subjectnonhuman
dc.subjectpriority journal
dc.subjectprotein interaction
dc.subjecttissue section
dc.subjectvirus attachment
dc.subjectvirus like agent
dc.titleMacrobrachium rosenbergii nodavirus virus-like particles attach to fucosylated glycans in the gills of the giant freshwater prawn
dc.typeArticle
dc.rights.holderScopus
dc.identifier.bibliograpycitationCellular Microbiology. Vol 22, No.12 (2020)
dc.identifier.doi10.1111/cmi.13258
Appears in Collections:Scopus 1983-2021

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