Quantitative proteomics analysis provides insight into the biological role of Hsp90 in BmNPV infection in Bombyx mori

Wu, Ping; Shang, Qi; Huang, Haoling; Zhang, Shaolun; Zhong, Jinbo; Hou, Qirui; Guo, Xijie

doi:10.1016/j.jprot.2019.103379

Cited by 23 publications

(20 citation statements)

References 55 publications

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“…Our findings are aligned with the previous research on DE circRNAs in midgut following BmNPV infection (Hu, Zhu, Liu, et al, 2018; Hu, Zhu, Zhang, et al, 2018). It is reported that the reproduction of BmNPV is highly dependent on host energy metabolism (Somu, Karuppiah, & Sundaram, 2019; Wu, Shang, Huang et al, 2019; Yu et al, 2017). The results revealed that those DE circRNAs affected metabolic balance during the process of virus infection.…”

Section: Discussionmentioning

confidence: 99%

Expression profile analysis of circular RNAs in BmN cells (Bombyx mori) upon BmNPV infection

Zhang

Shen

Yin

et al. 2020

Arch Insect Biochem Physiol

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The disease caused by Bombyx mori nucleopolyhedrovirus (BmNPV) has always been difficult to control, resulting in tremendous economic losses in the sericulture industry. Although much has been learned about the impact of noncoding RNAs on pathogenesis, the role of circular RNA (circRNA) in insect immunity remains unclear. To explore circRNA regulation involved in BmNPV infection, we used transcriptome analysis of BmN cells with or without BmNPV infection to generate circRNA data set. A total of 444 novel circRNAs were identified in BmN cells, with 198 pervasively distributed both in the control group and BmNPV-infection group. The host genes were enriched inMAPK signaling pathway, dorso-ventral axis formation, and ECM-receptor interaction, which were required for the normal larval growth. A total of 75 circRNAs were differentially expressed (DE) on BmNPV infection. Six downregulated circRNAs were validated by Sanger sequencing and qRT-PCR. DEcircRNA-miRNA-DEmRNA network was constructed based on the six validated cir-cRNAs. Pathway analysis indicated that the predicted target genes were mainly enriched in the metabolic pathway and immune-related signaling pathway. Our results may provide a basis for further studies on circRNA function in BmN cells challenged by BmNPV infection and offer an

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Section: Discussionmentioning

confidence: 99%

Expression profile analysis of circular RNAs in BmN cells (Bombyx mori) upon BmNPV infection

Zhang

Shen

Yin

et al. 2020

Arch Insect Biochem Physiol

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“…After 16 h of digestion at 37°C, peptides were desalted with a C18 cartridge to remove urea, and desalted peptides were dried by vacuum centrifugation. Desalted peptides were labeled with TMT6/10-plex reagents (TMT6/10plex™ Isobaric Label Reagent Set, Thermo Fisher) as previously described [52]. TMTlabeled peptide mix was fractionated using a C18 column (Waters BEH C18 4.6 × 250 mm, 5 μm; Waters Corporation, Milford, MA, USA) on a Rigol L3000 highperformance liquid chromatographer operating at 1 mL/ min, and the column oven was set at 50°C.…”

Section: Determination Of Mic and Antimicrobial Tolerance Of Strainsmentioning

confidence: 99%

ClpP participates in stress tolerance, biofilm formation, antimicrobial tolerance, and virulence of Enterococcus faecalis

Zheng

Wang

et al. 2020

BMC Microbiol

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Background: ClpP is important for bacterial growth and plays an indispensable role in cellular protein quality control systems by refolding or degrading damaged proteins, but the physiological significance of ClpP in Enterococcus faecalis remains obscure. A clpP deletion mutant (△clpP) was constructed using the E. faecalis OG1RF strain to clarify the effect of ClpP on E. faecalis. The global abundance of proteins was determined by a mass spectrometer with tandem mass tag labeling. Results: The ΔclpP mutant strain showed impaired growth at 20°C or 45°C at 5% NaCl or 2 mM H 2 O 2 . The number of surviving ΔclpP mutants decreased after exposure to the high concentration (50× minimal inhibitory concentration) of linezolid or minocycline for 96 h. The ΔclpP mutant strain also demonstrated decreased biofilm formation but increased virulence in a Galleria mellonella model. The mass spectrometry proteomics data indicated that the abundances of 135 proteins changed (111 increased, 24 decreased) in the ΔclpP mutant strain. Among those, the abundances of stress response or virulence relating proteins: FsrA response regulator, gelatinase GelE, regulatory protein Spx (spxA), heat-inducible transcription repressor HrcA, transcriptional regulator CtsR, ATPase/ chaperone ClpC, acetyl esterase/lipase, and chaperonin GroEL increased in the ΔclpP mutant strain; however, the abundances of ribosomal protein L4/L1 family protein (rplD), ribosomal protein L7/L12 (rplL2), 50S ribosomal protein L13 (rplM), L18 (rplR), L20 (rplT), 30S ribosomal protein S14 (rpsN2) and S18 (rpsR) all decreased. The abundances of biofilm formation-related adapter protein MecA increased, while the abundances of dihydroorotase (pyrC), orotate phosphoribosyltransferase (pyrE), and orotidine-5′-phosphate decarboxylase (pyrF) all decreased in the ΔclpP mutant strain. Conclusion:The present study demonstrates that ClpP participates in stress tolerance, biofilm formation, antimicrobial tolerance, and virulence of E. faecalis.

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“…Total DNA was extracted with a PureLink genomic DNA mini kit (Invitrogen) according to the manufacturer's instructions. In order to detect the relative expression of host genes in different treatments, relative RT-qPCR was performed as described in one of our previous studies (Wu et al, 2019b). In order to determine the BmNPV gene and vDNA synthesis amounts, absolute RT-qPCR was carried out as described in another of our previous studies (Wu et al, 2019a).…”

Section: Rt-qpcr Analysismentioning

confidence: 99%

Inhibition of heat shock protein 90 suppresses Bombyx mori nucleopolyhedrovirus replication in B. mori

Shang

Huang

et al. 2019

Insect Molecular Biology

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Heat shock protein 90 (Hsp90) plays a very important role in facilitating the replication of many viruses. Until now, little has been known about the role of Hsp90 in Bombyx mori virus infection. In this study, we explored the role of BmHsp90 in B. mori nucleopolyhedrovirus (BmNPV) replication. We found that BmHsp90 inhibition by geldanamycin (GA) significantly reduced the BmNPV titre, the protein expression level of BmNPV nucleocapsid protein 39 (VP39) and the transcript level of BmNPV genes. Silencing the hsp90 gene in BmN cells by small interfering RNA suppressed BmNPV replication whereas overexpression of hsp90 promoted the replication of BmNPV. After inhibition of Hsp90, the expression of three key genes [signal transducing activator of transcription (stat), suppressor of cytokine signalling protein 2 (socs2), socs6] involved in the Janus kinase/STAT pathway significantly changed, with up‐regulation of stat and down‐regulation of socs2 and socs6. In addition, the expression of two antiapoptosis genes, BmNPV inhibitor of apoptosis protein1 (BmNPV‐iap1) and Bmiap2, was greatly decreased in GA‐treated cells, whereas their expression was significantly increased in hsp90‐overexpressed silkworm larvae. Our results indicated that inhibition of Hsp90 can suppress BmNPV proliferation in B. mori. Our findings may provide new clues to elucidate the molecular mechanisms of silkworm–virus interactions.

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Quantitative proteomics analysis provides insight into the biological role of Hsp90 in BmNPV infection in Bombyx mori

Cited by 23 publications

References 55 publications

Expression profile analysis of circular RNAs in BmN cells (Bombyx mori) upon BmNPV infection

Expression profile analysis of circular RNAs in BmN cells (Bombyx mori) upon BmNPV infection

ClpP participates in stress tolerance, biofilm formation, antimicrobial tolerance, and virulence of Enterococcus faecalis

Inhibition of heat shock protein 90 suppresses Bombyx mori nucleopolyhedrovirus replication in B. mori

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