Screening and Identification of DnaJ Interaction Proteins in Streptococcus pneumoniae

Cai, Yingying; Yan, Wenjuan; Xu, Wenchun; Yin, Yibing; He, Yujuan; Wang, Hong; Zhang, Xuemei

doi:10.1007/s00284-013-0424-4

Cited by 3 publications

(4 citation statements)

References 35 publications

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“…They act as co‐chaperones in folding and assembly of newly synthesised proteins, aggregation prevention, dissolution and refolding of aggregated proteins, translocation of proteins across membranes and protein degradation (Cai et al . ; Kong et al . ).…”

Section: Resultsmentioning

confidence: 99%

“…The ubiquitous DnaJ proteins, which belong to the conserved HSP40 family, are involved in essential cellular functions. They act as co-chaperones in folding and assembly of newly synthesised proteins, aggregation prevention, dissolution and refolding of aggregated proteins, translocation of proteins across membranes and protein degradation (Cai et al 2013;Kong et al 2014). Yeast two-hybrid assay suggests that AtRBP45b could interact with molecular chaperone-containing proteins.…”

Section: Validation Of Atrbp45b Interactors Using Yeast Two-hybrid Anmentioning

confidence: 99%

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Interacting protein partners of Arabidopsis RNA‐binding protein AtRBP45b

Muthuramalingam

Wang

et al. 2017

Plant Biol J

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RNA binding proteins, important players in post-transcriptional gene regulation, usually exist in ribonuclear complexes. However, even in model systems like Arabidopsis characterisation of RBP associated proteins is limited. In this study, we investigated the interacting proteins of the Arabidopsis AtRBP45b, which is involved in stress signalling. In vivo localisation of AtRBP45b was conducted using 35S-GFP. FLAG-tagged AtRBP45b under control of the 35S promoter in the Atrbp45b-1 mutant background was used to pull down AtRBP45b interacting proteins. Yeast two-hybrid analysis, fluorescence energy resonance transfer assays were used to confirm the veracity of the AtRBP45b interacting proteins. In planta GFP-tagging indicated AtRBP45b is localised to the nucleus and the cytosol. AtRBP45b protein has a N-terminal proline-rich region and a C-terminal glutamine-rich domain that are usually involved in protein-protein interactions. Co-immunoprecipitation followed by mass spectrometry-based protein sequencing led to identification of 30 proteins that interacted with AtRBP45b. Using information from interactome databases (BIOGRID, INTACT and STRING), pull-down assays and localisation data, 12 putative interacting proteins were selected for yeast two-hybrid analysis. Cap-binding protein (CBP20, At5g44200) and polyA-binding protein (PAB8, At1g49760) were shown to interact with AtRBP45b. Based on its interacting partners we speculate that AtRBP45b may play an important role in RNA metabolism, especially in aspects related to mRNA stability and translation initiation during stress conditions in plants.

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Section: Resultsmentioning

confidence: 99%

Section: Validation Of Atrbp45b Interactors Using Yeast Two-hybrid Anmentioning

confidence: 99%

Interacting protein partners of Arabidopsis RNA‐binding protein AtRBP45b

Muthuramalingam

Wang

et al. 2017

Plant Biol J

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“…Prokaryotic heat-shock proteins (HSPs) are highly conserved molecular chaperones that are a virulence factor necessary for maintaining protein homeostasis during various stress processes. They contribute to bacterial attachment and invasion during the infections [14][15][16]. Pneumococcal DnaJ is a virulence factor belonging to a member of the HSP40 family [15].…”

Section: Introductionmentioning

confidence: 99%

“…They contribute to bacterial attachment and invasion during the infections [14][15][16]. Pneumococcal DnaJ is a virulence factor belonging to a member of the HSP40 family [15]. The main feature of this protein is the presence of a highly conserved J-domain, containing 70 amino acids in its Nterminus with four helical structures [17].…”

Section: Introductionmentioning

confidence: 99%

In-silico Analysis of Pneumococcal Heat-Shock Protein (DnaJ) to Predict Novel Multi-Epitope Vaccine Candidates

Afshari

Cohan²,

Sotoodehnejadnematalahi³

et al. 2021

vacres

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Introduction:To prevent pneumococcal infections, especially meningitis and bacteremia, and to overcome the serotype-dependent limitation of polysaccharide-based vaccines, the development of conserved protein-based vaccines is essential. This study aimed at investigate the in-silico analysis and epitope mapping of pneumococcal DnaJ for the first time, and to design the multi-epitope based vaccines with different categories by focusing on induction of both humoral and cellular immunities. Methods: We predicted B-and T-cell epitopes, IL-4, IL-17, IL-10, and IFN-γ inducer epitopes of DnaJ using Immunoinformatics tools. The immunogenicity and conservation score of the predicted epitopes among pneumococcal prevalent clinical serotypes, the immune simulation of DnaJ administration in mammals and potential regions involved in DnaJ-TLRs interactions were analyzed. Finally, we proposed three classes of multi-epitope DnaJ-based vaccine candidates. Results: This protein had 24 and 15 predicted linear Bcell and helper T-cell epitopes, respectively, with a conservation score of 86-100% among prevalent clinical pneumococcal serotypes. DnaJ also had many IL-4 and IFN-γ inducing epitopes and was considered an IL-10 and IL-17 inducer protein. The immune simulation showed induction of both humoral and cellular immunity against DnaJ. The residues at positions 274, 280, 292, 297, 300, 316-319, 333, 336-340, 358, 363-366, and 372 were predicted to be involved in DnaJ-TLR2 and DnaJ-TLR4 interactions. Three classes of proposed DnaJ-based constructs were based on only B-cell epitopes, only helper T-cell epitopes, and multi-epitopes of B-and T-cell and IL-17 epitopes. Conclusion:The results showed that although DnaJ has been reported to play an important role in cellular immunity, our results indicated the high potential of DnaJ to stimulate mucosal, humoral, and cellular immunity.

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Heat Shock Protein DnaJ in Pseudomonas aeruginosa Affects Biofilm Formation via Pyocyanin Production

et al. 2020

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Heat shock proteins (HSPs) play important biological roles, and they are implicated in bacterial response to environmental stresses and in pathogenesis of infection. The role of HSPs in P. aeruginosa, however, remains to be fully elucidated. Here, we report the unique role of HSP DnaJ in biofilm formation and pathogenicity in P. aeruginosa. A dnaJ mutant produced hardly any pyocyanin and formed significantly less biofilms, which contributed to decreased pathogenicity as demonstrated by reduced mortality rate in a Drosophila melanogaster infection model. The reduced pyocyanin production in the dnaJ mutant was a result of the decreased transcription of phenazine synthesis operons including phzA1, phzA2, phzS, and phzM. The reduction of biofilm formation and initial adhesion in the dnaJ mutant could be reversed by exogenously added pyocyanin or extracellular DNA (eDNA). Consistent with such observations, absence of dnaJ significantly reduced the release of eDNA in P. aeruginosa and addition of exogenous pyocyanin could restore eDNA release. These results indicate dnaJ mutation caused reduced pyocyanin production, which in turn caused the decreased eDNA, resulting in decreased biofilm formation. DnaJ is required for pyocyanin production and full virulence in P. aeruginosa; it affects biofilm formation and initial adhesion via pyocyanin, inducing eDNA release.

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Screening and Identification of DnaJ Interaction Proteins in Streptococcus pneumoniae

Cited by 3 publications

References 35 publications

Interacting protein partners of Arabidopsis RNA‐binding protein AtRBP45b

Interacting protein partners of Arabidopsis RNA‐binding protein AtRBP45b

In-silico Analysis of Pneumococcal Heat-Shock Protein (DnaJ) to Predict Novel Multi-Epitope Vaccine Candidates

Heat Shock Protein DnaJ in Pseudomonas aeruginosa Affects Biofilm Formation via Pyocyanin Production

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