Please use this identifier to cite or link to this item: https://ir.swu.ac.th/jspui/handle/123456789/12725
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dc.contributor.authorMatjank W.
dc.contributor.authorPonprateep S.
dc.contributor.authorRimphanitchayakit V.
dc.contributor.authorTassanakajon A.
dc.contributor.authorSomboonwiwat K.
dc.contributor.authorVatanavicharn T.
dc.date.accessioned2021-04-05T03:05:17Z-
dc.date.available2021-04-05T03:05:17Z-
dc.date.issued2018
dc.identifier.issn0145305X
dc.identifier.other2-s2.0-85053082050
dc.identifier.urihttps://ir.swu.ac.th/jspui/handle/123456789/12725-
dc.identifier.urihttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85053082050&doi=10.1016%2fj.dci.2018.07.021&partnerID=40&md5=d8dfaab4037163415ab32e7d3d2fd25a
dc.description.abstractPlasmolipin has been characterized as a cell entry receptor for mouse endogenous retrovirus. In black tiger shrimp, two isoforms of plasmolipin genes, PmPLP1 and PmPLP2, have been identified from the Penaeus monodon EST database. The PmPLP1 is highly up-regulated in yellow head virus (YHV)-infected shrimp. Herein, the function of PmPLP1 is shown to be involved in YHV infection. The immunoblotting and immunolocalization showed that the PmPLP1 protein was highly expressed and located at the plasma membrane of gills from YHV-infected shrimp. Moreover, the PmPLP1 expressed in the Sf9 insect cells resided at the cell membrane rendering the cells more susceptible to YHV infection. Using the ELISA binding and mortality assays, the synthetic external loop of PmPLP1 was shown to bind the purified YHV and neutralize the virus resulting in the decrease in YHV infection. Our results suggested that the PmPLP1 was likely a receptor of YHV in shrimp. © 2018 Elsevier Ltd
dc.subjectprotein plasmolipin
dc.subjectprotein PLP1
dc.subjectproteolipid protein
dc.subjectunclassified drug
dc.subjectarthropod protein
dc.subjectmyelin and lymphocyte protein
dc.subjectprotein binding
dc.subjectArticle
dc.subjectcell membrane
dc.subjectcontrolled study
dc.subjectdisease predisposition
dc.subjectenzyme linked immunosorbent assay
dc.subjectimmunoblotting
dc.subjectimmunolocalization
dc.subjectmortality rate
dc.subjectnonhuman
dc.subjectPenaeus monodon
dc.subjectpriority journal
dc.subjectprotein expression
dc.subjectprotein function
dc.subjectSf9 cell line
dc.subjectvirus neutralization
dc.subjectvirus purification
dc.subjectYellow head virus
dc.subjectanimal
dc.subjectblood cell
dc.subjectcytology
dc.subjectgill
dc.subjectimmunology
dc.subjectmetabolism
dc.subjectNidovirales infection
dc.subjectPenaeidae
dc.subjectRoniviridae
dc.subjectSpodoptera
dc.subjectupregulation
dc.subjectveterinary medicine
dc.subjectvirology
dc.subjectAnimals
dc.subjectArthropod Proteins
dc.subjectCell Membrane
dc.subjectGills
dc.subjectHemocytes
dc.subjectMyelin and Lymphocyte-Associated Proteolipid Proteins
dc.subjectNidovirales Infections
dc.subjectPenaeidae
dc.subjectProtein Binding
dc.subjectRoniviridae
dc.subjectSf9 Cells
dc.subjectSpodoptera
dc.subjectUp-Regulation
dc.titlePlasmolipin, PmPLP1, from Penaeus monodon is a potential receptor for yellow head virus infection
dc.typeArticle
dc.rights.holderScopus
dc.identifier.bibliograpycitationDevelopmental and Comparative Immunology. Vol 88, (2018), p.137-143
dc.identifier.doi10.1016/j.dci.2018.07.021
Appears in Collections:Scopus 1983-2021

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