Publication:
Silencing of a Kazal-type serine proteinase inhibitor SPIPm2 from Penaeus monodon affects YHV susceptibility and hemocyte homeostasis

dc.contributor.authorVisetnan S.
dc.contributor.authorDonpudsa S.
dc.contributor.authorTassanakajon A.
dc.contributor.authorRimphanitchayakit V.
dc.date.accessioned2021-04-05T03:21:39Z
dc.date.available2021-04-05T03:21:39Z
dc.date.issued2018
dc.date.issuedBE2561
dc.description.abstractIn shrimp, the Kazal-type serine proteinase inhibitors (KPIs) are involved in host innate immune defense system against pathogenic microorganisms. A five-Kazal-domain SPIPm2 is the most abundant KPIs in the black tiger shrimp Penaeus monodon and up-regulated in response to yellow head virus (YHV) infection. In this study, the role of SPIPm2 in YHV infection was investigated. The expression of SPIPm2 in hemocytes, gill and heart from 48-h YHV-infected shrimp was increased. The expression of SPIPm2 in hemocytes was significantly increased after 12 h of infection and gradually increased higher afterwards. Silencing of SPIPm2 by dsRNA interference resulted in the increased expression of different apoptosis-related genes, the increased expression of transcriptional factors of antimicrobial synthesis pathways, the reduction of circulating hemocytes in the shrimp hemolymph, and the increased susceptibility of the silenced shrimp to YHV infection. The activities of caspase-3 and caspase-7 in the hemocytes of SPIPm2-silenced shrimp was also increased by 5.32-fold as compared with those of the control shrimp. The results suggested that the SPIPm2 was involved in the hemocyte homeostasis. © 2018
dc.format.mimetypeapplication/pdf
dc.identifier.citationFish and Shellfish Immunology. Vol 79, (2018), p.18-27
dc.identifier.doi10.1016/j.fsi.2018.05.004
dc.identifier.issn10504648
dc.identifier.other2-s2.0-85046674536
dc.identifier.urihttps://swu-dspace2.eval.plus/handle/123456789/3732
dc.rights.holderScopus
dc.subject.otherALFPm3 protein
dc.subject.otherArthropod protein
dc.subject.otherCaspase 3
dc.subject.otherCaspase 7
dc.subject.otherCrustinPm1 protein
dc.subject.otherCrustinPm7 protein
dc.subject.otherCyclophilin A
dc.subject.otherDouble stranded RNA
dc.subject.otherKazal type serine proteinase inhibitor SPIPm2
dc.subject.otherPenaeidin3 protein
dc.subject.otherPenaeidin5 protein
dc.subject.otherPmDorsal protein
dc.subject.otherPmHHAP protein
dc.subject.otherPmIAP protein
dc.subject.otherPmKunitz protein
dc.subject.otherPmPO1 protein
dc.subject.otherPmPO2 protein
dc.subject.otherPmPPAE1 protein
dc.subject.otherPmPPAE2 protein
dc.subject.otherPmRelish protein
dc.subject.otherPmToll protein
dc.subject.otherSerine peptidase inhibitor Kazal type
dc.subject.otherSPIPm5 protein
dc.subject.otherSWDPm2 protein
dc.subject.otherTranscription factor
dc.subject.otherUnclassified drug
dc.subject.otherArthropod protein
dc.subject.otherSerine peptidase inhibitor Kazal type
dc.subject.otherAnimal experiment
dc.subject.otherAnimal tissue
dc.subject.otherApoptosis
dc.subject.otherArticle
dc.subject.otherBlood cell
dc.subject.otherControlled study
dc.subject.otherDisease predisposition
dc.subject.otherDown regulation
dc.subject.otherEnzyme activity
dc.subject.otherGene expression
dc.subject.otherGene knockdown
dc.subject.otherGene silencing
dc.subject.otherGill
dc.subject.otherHeart
dc.subject.otherHemolymph
dc.subject.otherHomeostasis
dc.subject.otherImmune-related gene
dc.subject.otherInnate immunity
dc.subject.otherMortality rate
dc.subject.otherNidovirales infection
dc.subject.otherNonhuman
dc.subject.otherPenaeus monodon
dc.subject.otherPriority journal
dc.subject.otherProtein function
dc.subject.otherReal time polymerase chain reaction
dc.subject.otherRNA interference
dc.subject.otherTissue distribution
dc.subject.otherUpregulation
dc.subject.otherYellow head virus
dc.subject.otherAnimal
dc.subject.otherBlood cell
dc.subject.otherCardiac muscle
dc.subject.otherGene expression profiling
dc.subject.otherGenetics
dc.subject.otherImmunology
dc.subject.otherMetabolism
dc.subject.otherPenaeidae
dc.subject.otherPhysiology
dc.subject.otherRoniviridae
dc.subject.otherVirology
dc.subject.otherAnimals
dc.subject.otherArthropod Proteins
dc.subject.otherGene Expression Profiling
dc.subject.otherGene Silencing
dc.subject.otherGills
dc.subject.otherHeart
dc.subject.otherHemocytes
dc.subject.otherMyocardium
dc.subject.otherPenaeidae
dc.subject.otherRoniviridae
dc.subject.otherSerine Peptidase Inhibitors, Kazal Type
dc.titleSilencing of a Kazal-type serine proteinase inhibitor SPIPm2 from Penaeus monodon affects YHV susceptibility and hemocyte homeostasis
dc.typeArticle
dspace.entity.typePublication
swu.datasource.scopushttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85046674536&doi=10.1016%2fj.fsi.2018.05.004&partnerID=40&md5=f4eee8ca802d7cba31aa3269b5cc9c1e

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