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Macrobrachium rosenbergii nodavirus virus-like particles attach to fucosylated glycans in the gills of the giant freshwater prawn

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dc.contributor.author Somrit M.
dc.contributor.author Yu S.-Y.
dc.contributor.author Le Pendu J.
dc.contributor.author Breiman A.
dc.contributor.author Guérardel Y.
dc.contributor.author Weerachatyanukul W.
dc.contributor.author Watthammawut A.
dc.date.accessioned 2021-04-05T03:03:22Z
dc.date.available 2021-04-05T03:03:22Z
dc.date.issued 2020
dc.identifier.issn 14625814
dc.identifier.other 2-s2.0-85090950583
dc.identifier.uri https://ir.swu.ac.th/jspui/handle/123456789/12432
dc.identifier.uri https://www.scopus.com/inward/record.uri?eid=2-s2.0-85090950583&doi=10.1111%2fcmi.13258&partnerID=40&md5=6ed4b7fc0937abca60c9f40d3a25124f
dc.description.abstract The 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.rights Srinakharinwirot University
dc.subject fucose
dc.subject glycan
dc.subject glycoprotein
dc.subject lectin
dc.subject periodate
dc.subject Aleuria aurantia
dc.subject animal cell
dc.subject animal tissue
dc.subject Article
dc.subject binding site
dc.subject cell lysate
dc.subject controlled study
dc.subject freshwater species
dc.subject fucosylation
dc.subject gill
dc.subject Macrobrachium rosenbergii
dc.subject mass spectrometry
dc.subject Nodaviridae
dc.subject nonhuman
dc.subject priority journal
dc.subject protein interaction
dc.subject tissue section
dc.subject virus attachment
dc.subject virus like agent
dc.title Macrobrachium rosenbergii nodavirus virus-like particles attach to fucosylated glycans in the gills of the giant freshwater prawn
dc.type Article
dc.rights.holder Scopus
dc.identifier.bibliograpycitation Cellular Microbiology. Vol 22, No.12 (2020)
dc.identifier.doi 10.1111/cmi.13258


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