<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Wang C</submitter><funding>National Natural Science Foundation of China (CN)</funding><funding>National Natural Science Foundation of China</funding><pagination>102</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC6389150</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>49(1)</volume><pubmed_abstract>Many viral proteins are related to suppressing apoptosis in target cells and are hence beneficial to viral replication. The V protein of Newcastle disease virus (NDV) is one such protein that plays an important role in inhibiting apoptosis in a species-specific manner. However, to date, there have been no reports clarifying the antiapoptotic mechanisms of the V protein. The present study was undertaken to determine the apoptotic potential of the V protein in a chicken embryo fibroblast cell line (DF-1 cell) and to elucidate its molecular mechanisms of action. Here, a yeast two-hybrid system was used to screen the host proteins that interact with the V protein and identified thioredoxin-like protein 1 (TXNL1) as a potential binding partner. Immuno-colocalization of V protein and TXNL1 protein in DF-1 cells further verified the interaction of the two proteins. Through the overexpression of TXNL1 protein and knockdown of TXNL1 protein in DF-1 cells, the effects of NDV replication and cell apoptosis were examined. Cell apoptosis was detected by flow cytometry. The mRNA and protein expression levels of Bax, Bcl-2 and Caspase-3 were detected by quantitative real-time PCR (Q-PCR) and Western blotting. NDV expression was detected by Q-PCR and plaque assay. The results revealed that the TXNL1 protein induced apoptosis and inhibited NDV replication in DF-1 cells. Furthermore, the Western blot and Q-PCR results suggested that TXNL1 induced cell apoptosis through a pathway involving Bcl-2\Bax and Caspase-3. Finally, this work provides insight into the mechanism by which the V protein inhibits apoptosis.</pubmed_abstract><journal>Veterinary research</journal><pubmed_title>Newcastle disease virus V protein inhibits apoptosis in DF-1 cells by downregulating TXNL1.</pubmed_title><pmcid>PMC6389150</pmcid><funding_grant_id>31572538</funding_grant_id><pubmed_authors>Adam FEA</pubmed_authors><pubmed_authors>Wang C</pubmed_authors><pubmed_authors>Chu Z</pubmed_authors><pubmed_authors>Pang Y</pubmed_authors><pubmed_authors>Xiao S</pubmed_authors><pubmed_authors>Liu W</pubmed_authors><pubmed_authors>Lu K</pubmed_authors><pubmed_authors>Yang Z</pubmed_authors><pubmed_authors>Tang Q</pubmed_authors><pubmed_authors>Ma J</pubmed_authors><pubmed_authors>Gao X</pubmed_authors><pubmed_authors>Dang R</pubmed_authors><pubmed_authors>Wang X</pubmed_authors></additional><is_claimable>false</is_claimable><name>Newcastle disease virus V protein inhibits apoptosis in DF-1 cells by downregulating TXNL1.</name><description>Many viral proteins are related to suppressing apoptosis in target cells and are hence beneficial to viral replication. The V protein of Newcastle disease virus (NDV) is one such protein that plays an important role in inhibiting apoptosis in a species-specific manner. However, to date, there have been no reports clarifying the antiapoptotic mechanisms of the V protein. The present study was undertaken to determine the apoptotic potential of the V protein in a chicken embryo fibroblast cell line (DF-1 cell) and to elucidate its molecular mechanisms of action. Here, a yeast two-hybrid system was used to screen the host proteins that interact with the V protein and identified thioredoxin-like protein 1 (TXNL1) as a potential binding partner. Immuno-colocalization of V protein and TXNL1 protein in DF-1 cells further verified the interaction of the two proteins. Through the overexpression of TXNL1 protein and knockdown of TXNL1 protein in DF-1 cells, the effects of NDV replication and cell apoptosis were examined. Cell apoptosis was detected by flow cytometry. The mRNA and protein expression levels of Bax, Bcl-2 and Caspase-3 were detected by quantitative real-time PCR (Q-PCR) and Western blotting. NDV expression was detected by Q-PCR and plaque assay. The results revealed that the TXNL1 protein induced apoptosis and inhibited NDV replication in DF-1 cells. Furthermore, the Western blot and Q-PCR results suggested that TXNL1 induced cell apoptosis through a pathway involving Bcl-2\Bax and Caspase-3. Finally, this work provides insight into the mechanism by which the V protein inhibits apoptosis.</description><dates><release>2018-01-01T00:00:00Z</release><publication>2018 Oct</publication><modification>2024-11-21T07:27:39.316Z</modification><creation>2019-06-06T20:54:05Z</creation></dates><accession>S-EPMC6389150</accession><cross_references><pubmed>30290847</pubmed><doi>10.1186/s13567-018-0599-6</doi></cross_references></HashMap>