Characterization of X- box binding protein 1(XBP1) and BiP functions and investigation their roles in YHV replication in P. monodon

Eukaryotic cells have mechanisms to cope with stress in endoplasmic reticulum (ER) called unfolded protein response (UPR). In this study, we characterized putative X-box DNA binding protein1 (XBP1) and Binding protein (BiP) cDNAs from black tiger shrimp (Peneaus monodon). When the shrimp were infect...

Full description

Saved in:
Bibliographic Details
Main Authors: Piyawadee Rugsanit, Pongsopee Attasart, Apinunt Udomkit, Witoon Tirasophon
Other Authors: Institute of Molecular Biosciences, Mahidol University
Format: Article
Published: 2022
Subjects:
Online Access:https://repository.li.mahidol.ac.th/handle/123456789/79303
Tags: Add Tag
No Tags, Be the first to tag this record!
Institution: Mahidol University
id th-mahidol.79303
record_format dspace
spelling th-mahidol.793032022-08-04T18:39:52Z Characterization of X- box binding protein 1(XBP1) and BiP functions and investigation their roles in YHV replication in P. monodon Piyawadee Rugsanit Pongsopee Attasart Apinunt Udomkit Witoon Tirasophon Institute of Molecular Biosciences, Mahidol University Multidisciplinary Eukaryotic cells have mechanisms to cope with stress in endoplasmic reticulum (ER) called unfolded protein response (UPR). In this study, we characterized putative X-box DNA binding protein1 (XBP1) and Binding protein (BiP) cDNAs from black tiger shrimp (Peneaus monodon). When the shrimp were infected with Yellow head virus (YHV), the level of XBP1 and BiP mRNA transcript were elevated approximately 8 and 55 folds, respectively. In normal shrimp, the putative XBP1 (XBP1u) was predicted to encode a protein with 283 amino acid residues. When shrimp were infected with YHV, portion of cDNA with17 nucleotides intron elimination (XBP1s) was observed. The elimination cause alteration of its translational frame. The predicted protein from this is 469 amino acids in length with totally change in its amino acid sequence downstream of the intron. Functional analysis of these XBP1 proteins in mammalian cells clearly showed that overexpression of P. monodon XBP1s was capable of activating the transcription rate of mammalian UPR responsive genes (BiP, ERdj4 and P58IPK). Finally, the impact of XBP1 and BiP on YHV multiplication in black tiger shrimp was investigated by RNAi approach. Knocking down either XBP1 or BiP expression efficiently inhibited YHV replication. Therefore, these two components in the UPR pathway may be an interesting target for anti YHV development in the future. 2022-08-04T11:39:52Z 2022-08-04T11:39:52Z 2021-10-01 Article Chiang Mai University Journal of Natural Sciences. Vol.20, No.4 (2021), 1-15 10.12982/CMUJNS.2021.090 16851994 2-s2.0-85115358263 https://repository.li.mahidol.ac.th/handle/123456789/79303 Mahidol University SCOPUS https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=85115358263&origin=inward
institution Mahidol University
building Mahidol University Library
continent Asia
country Thailand
Thailand
content_provider Mahidol University Library
collection Mahidol University Institutional Repository
topic Multidisciplinary
spellingShingle Multidisciplinary
Piyawadee Rugsanit
Pongsopee Attasart
Apinunt Udomkit
Witoon Tirasophon
Characterization of X- box binding protein 1(XBP1) and BiP functions and investigation their roles in YHV replication in P. monodon
description Eukaryotic cells have mechanisms to cope with stress in endoplasmic reticulum (ER) called unfolded protein response (UPR). In this study, we characterized putative X-box DNA binding protein1 (XBP1) and Binding protein (BiP) cDNAs from black tiger shrimp (Peneaus monodon). When the shrimp were infected with Yellow head virus (YHV), the level of XBP1 and BiP mRNA transcript were elevated approximately 8 and 55 folds, respectively. In normal shrimp, the putative XBP1 (XBP1u) was predicted to encode a protein with 283 amino acid residues. When shrimp were infected with YHV, portion of cDNA with17 nucleotides intron elimination (XBP1s) was observed. The elimination cause alteration of its translational frame. The predicted protein from this is 469 amino acids in length with totally change in its amino acid sequence downstream of the intron. Functional analysis of these XBP1 proteins in mammalian cells clearly showed that overexpression of P. monodon XBP1s was capable of activating the transcription rate of mammalian UPR responsive genes (BiP, ERdj4 and P58IPK). Finally, the impact of XBP1 and BiP on YHV multiplication in black tiger shrimp was investigated by RNAi approach. Knocking down either XBP1 or BiP expression efficiently inhibited YHV replication. Therefore, these two components in the UPR pathway may be an interesting target for anti YHV development in the future.
author2 Institute of Molecular Biosciences, Mahidol University
author_facet Institute of Molecular Biosciences, Mahidol University
Piyawadee Rugsanit
Pongsopee Attasart
Apinunt Udomkit
Witoon Tirasophon
format Article
author Piyawadee Rugsanit
Pongsopee Attasart
Apinunt Udomkit
Witoon Tirasophon
author_sort Piyawadee Rugsanit
title Characterization of X- box binding protein 1(XBP1) and BiP functions and investigation their roles in YHV replication in P. monodon
title_short Characterization of X- box binding protein 1(XBP1) and BiP functions and investigation their roles in YHV replication in P. monodon
title_full Characterization of X- box binding protein 1(XBP1) and BiP functions and investigation their roles in YHV replication in P. monodon
title_fullStr Characterization of X- box binding protein 1(XBP1) and BiP functions and investigation their roles in YHV replication in P. monodon
title_full_unstemmed Characterization of X- box binding protein 1(XBP1) and BiP functions and investigation their roles in YHV replication in P. monodon
title_sort characterization of x- box binding protein 1(xbp1) and bip functions and investigation their roles in yhv replication in p. monodon
publishDate 2022
url https://repository.li.mahidol.ac.th/handle/123456789/79303
_version_ 1763495829111308288