PXD004748

PXD004748 is an original dataset announced via ProteomeXchange.

Title	Dynamics of the interaction between cotton bollworm Helicoverpa armigera and nucleopolyhedrovirus as revealed by integrated transcriptomic and proteomic analyses
Description	Over the past decades, Helicoverpa armigera nucleopolyhedrovirus (HearNPV) has been widely used for biocontrol of cotton bollworm, which is one of the most destructive pest insects in agriculture worldwide. However, the molecular mechanism underlying the interaction between HearNPV and host insects remains poorly understood. In this study, high throughput RNA-sequencing was integrated with label-free quantitative proteomics analysis to examine the dynamics of gene expression in the fat body of H. armigera larvae in response to challenge with HearNPV. RNA-sequencing-based transcriptomic analysis indicated that host gene expression was substantially altered, yielding 3,850 differentially expressed genes (DEGs), while no global transcriptional shut-off effects were observed in the fat body. Among the DEGs, 60 immunity-related genes were down-regulated after baculovirus infection, a finding that was consistent with the results of quantitative real-time RT-PCR (qRT-PCR). Gene ontology and functional classification demonstrated that the majority of down-regulated genes were enriched in gene cohorts involved in energy, carbohydrate, and amino acid metabolic pathways. Proteomics analysis identified differentially expressed proteins in the fat body, among which 76 were up-regulated, whereas 373 were significantly down-regulated upon infection. The down-regulated proteins are involved in metabolic pathways such as energy metabolism, carbohydrate metabolism (CM), and amino acid metabolism, in agreement with the RNA-seq data. Furthermore, correlation analysis suggested a strong association between the mRNA level and protein abundance in the H. armigera fat body. More importantly, the predicted gene interaction network indicated that a large subset of metabolic networks was significantly negatively regulated by viral infection, including CM-related enzymes such as aldolase, enolase, malate dehydrogenase and triose-phosphate isomerase. Taken together, transcriptomic combined with proteomic data elucidated that baculovirus established systemic infection of host larvae, and manipulated the host mainly by suppressing the host immune response and down-regulating metabolism to allow viral self-replication and proliferation. Therefore, this study provided important insights into the mechanism of host-baculovirus interaction.
HostingRepository	PRIDE
AnnounceDate	2024-10-22
AnnouncementXML	Submission_2024-10-22_04:32:07.775.xml
DigitalObjectIdentifier
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Unsupported dataset by repository
PrimarySubmitter	Zhen Zou
SpeciesList	scientific name: Helicoverpa armigera (Cotton bollworm); NCBI TaxID: 29058;
ModificationList	monohydroxylated residue; acetylated residue; iodoacetamide derivatized residue
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2016-08-10 04:18:51	ID requested
1	2017-04-19 06:50:06	announced
⏵ 2	2024-10-22 04:32:08	announced	2024-10-22: Updated project metadata.

Xing L, Yuan C, Wang M, Lin Z, Shen B, Hu Z, Zou Z, and Nucleopolyhedrovirus as Revealed by Integrated Transcriptomic and Proteomic Analyses. Mol Cell Proteomics, 16(6):1009-1028(2017) [pubmed]

10.1074/mcp.M116.062547;

curator keyword: Biological

submitter keyword: Cotton bollworm, insect immunity, carbohydrate metabolism, baculovirus, host-pathogen interaction, fat body, RNA-seq, LC-MS/MS

Zhen Zou
contact affiliation	Institute of Zoology, Chinese Academy of Sciences
contact email	zouzhen@ioz.ac.cn
lab head
Zhen Zou
contact affiliation	Institute of Zoology, CAS
contact email	zouzhen@ioz.ac.cn
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD004748
     1. Label: PRIDE project
     2. Name: Dynamics of the interaction between cotton bollworm Helicoverpa armigera and nucleopolyhedrovirus as revealed by integrated transcriptomic and proteomic analyses