Sodium butyrate modulates chicken macrophage proteins essential for Salmonella Enteritidis invasion

Salmonella Enteritidis is an intracellular foodborne pathogen that has developed multiple mechanisms to alter poultry intestinal physiology and infect the gut. Short chain fatty acid butyrate is derived from microbiota metabolic activities, and it maintains gut homeostasis. There is limited understanding on the interaction between S. Enteritidis infection, butyrate, and host intestinal response. To fill this knowledge gap, chicken macrophages (also known as HTC cells) were infected with S. Enteritidis, treated with sodium butyrate, and proteomic analysis was performed. A growth curve assay was conducted to determine sub-inhibitory concentration (SIC, concentration that do not affect bacterial growth compared to control) of sodium butyrate against S. Enteritidis. HTC cells were infected with S. Enteritidis in the presence and absence of SIC of sodium butyrate. The proteins were extracted and analyzed by tandem mass spectrometry. Our results showed that the SIC was 45 mM. Notably, S. Enteritidis-infected HTC cells upregulated macrophage proteins involved in ATP synthesis through oxidative phosphorylation such as ATP synthase subunit alpha (ATP5A1), ATP synthase subunit d, mitochondrial (ATP5PD) and cellular apoptosis such as Cytochrome-c (CYC). Furthermore, sodium butyrate influenced S. Enteritidis-infected HTC cells by reducing the expression of macrophage proteins mediating actin cytoskeletal rearrangements such as WD repeat-containing protein-1 (WDR1), Alpha actinin-1 (ACTN1), Vinculin (VCL) and Protein disulfide isomerase (P4HB) and intracellular S. Enteritidis growth and replication such as V-type proton ATPase catalytic subunit A (ATPV1A). Interestingly, sodium butyrate increased the expression of infected HTC cell protein involving in bacterial killing such as Vimentin (VIM). In conclusion, sodium butyrate modulates the expression of HTC cell proteins essential for S. Enteritidis invasion.

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The Campylobacter jejuni CiaD effector co-opts the host cell protein IQGAP1 to promote cell entry

Nature Communications ◽

10.1038/s41467-021-21579-5 ◽

2021 ◽

Vol 12 (1) ◽

Author(s):

Nicholas M. Negretti ◽

Christopher R. Gourley ◽

Prabhat K. Talukdar ◽

Geremy Clair ◽

Courtney M. Klappenbach ◽

...

Keyword(s):

Host Cell ◽

Campylobacter Jejuni ◽

Foodborne Pathogen ◽

Small Gtpase ◽

Host Cells ◽

Cell Protein ◽

Host Cell Protein ◽

Cell Binding ◽

Actin Reorganization ◽

Cell Cytosol

AbstractCampylobacter jejuni is a foodborne pathogen that binds to and invades the epithelial cells lining the human intestinal tract. Maximal invasion of host cells by C. jejuni requires cell binding as well as delivery of the Cia proteins (Campylobacter invasion antigens) to the host cell cytosol via the flagellum. Here, we show that CiaD binds to the host cell protein IQGAP1 (a Ras GTPase-activating-like protein), thus displacing RacGAP1 from the IQGAP1 complex. This, in turn, leads to the unconstrained activity of the small GTPase Rac1, which is known to have roles in actin reorganization and internalization of C. jejuni. Our results represent the identification of a host cell protein targeted by a flagellar secreted effector protein and demonstrate that C. jejuni-stimulated Rac signaling is dependent on IQGAP1.

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Rates of various reactions catalyzed by ATP synthase as related to the mechanism of ATP synthesis.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)52411-x ◽

1991 ◽

Vol 266 (1) ◽

pp. 123-129

Author(s):

D A Berkich ◽

G D Williams ◽

P T Masiakos ◽

M B Smith ◽

P D Boyer ◽

...

Keyword(s):

Atp Synthase ◽

Atp Synthesis

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Carbon and Nitrogen Sources Have No Impact on the Organization and Composition of Ustilago maydis Respiratory Supercomplexes

Journal of Fungi ◽

10.3390/jof7010042 ◽

2021 ◽

Vol 7 (1) ◽

pp. 42

Author(s):

Deyamira Matuz-Mares ◽

Oscar Flores-Herrera ◽

Guadalupe Guerra-Sánchez ◽

Lucero Romero-Aguilar ◽

Héctor Vázquez-Meza ◽

...

Keyword(s):

Atp Synthase ◽

Polyacrylamide Gel Electrophoresis ◽

Atp Synthesis ◽

Nitrogen Sources ◽

Growth Conditions ◽

Energy Conditions ◽

Respiratory Complexes ◽

Respiratory Supercomplexes ◽

Nadh Dehydrogenases ◽

Reduced Nicotinamide Adenine Dinucleotide

Respiratory supercomplexes are found in mitochondria of eukaryotic cells and some bacteria. A hypothetical role of these supercomplexes is electron channeling, which in principle should increase the respiratory chain efficiency and ATP synthesis. In addition to the four classic respiratory complexes and the ATP synthase, U. maydis mitochondria contain three type II NADH dehydrogenases (NADH for reduced nicotinamide adenine dinucleotide) and the alternative oxidase. Changes in the composition of the respiratory supercomplexes due to energy requirements have been reported in certain organisms. In this study, we addressed the organization of the mitochondrial respiratory complexes in U. maydis under diverse energy conditions. Supercomplexes were obtained by solubilization of U. maydis mitochondria with digitonin and separated by blue native polyacrylamide gel electrophoresis (BN-PAGE). The molecular mass of supercomplexes and their probable stoichiometries were 1200 kDa (I1:IV1), 1400 kDa (I1:III2), 1600 kDa (I1:III2:IV1), and 1800 kDa (I1:III2:IV2). Concerning the ATP synthase, approximately half of the protein is present as a dimer and half as a monomer. The distribution of respiratory supercomplexes was the same in all growth conditions. We did not find evidence for the association of complex II and the alternative NADH dehydrogenases with other respiratory complexes.

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Boric Acid‐Fueled ATP Synthesis by FoF1 ATP Synthase Reconstituted in a Supramolecular Architecture

Angewandte Chemie ◽

10.1002/ange.202016253 ◽

2020 ◽

Author(s):

Junbai Li ◽

Xia Xu ◽

Jinbo Fei ◽

Youqian Xu ◽

Guangle Li ◽

...

Keyword(s):

Boric Acid ◽

Atp Synthase ◽

Atp Synthesis ◽

Supramolecular Architecture ◽

Fof1 Atp Synthase

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Crystallographic structure of the turbine C-ring from spinach chloroplast F-ATP synthase

Bioscience Reports ◽

10.1042/bsr20130114 ◽

2014 ◽

Vol 34 (2) ◽

Cited By ~ 4

Author(s):

Asha Manikkoth Balakrishna ◽

Holger Seelert ◽

Sven-Hendric Marx ◽

Norbert A. Dencher ◽

Gerhard Grüber

Keyword(s):

Atp Synthase ◽

Ring Width ◽

Atp Synthesis ◽

Crystallographic Structure ◽

Unit Cell Parameters ◽

Subunit C ◽

Cell Parameters ◽

Ring Diameter ◽

C Subunit

In eukaryotic and prokaryotic cells, F-ATP synthases provide energy through the synthesis of ATP. The chloroplast F-ATP synthase (CF1FO-ATP synthase) of plants is integrated into the thylakoid membrane via its FO-domain subunits a, b, b’ and c. Subunit c with a stoichiometry of 14 and subunit a form the gate for H+-pumping, enabling the coupling of electrochemical energy with ATP synthesis in the F1 sector. Here we report the crystallization and structure determination of the c14-ring of subunit c of the CF1FO-ATP synthase from spinach chloroplasts. The crystals belonged to space group C2, with unit-cell parameters a=144.420, b=99.295, c=123.51 Å, and β=104.34° and diffracted to 4.5 Å resolution. Each c-ring contains 14 monomers in the asymmetric unit. The length of the c-ring is 60.32 Å, with an outer ring diameter 52.30 Å and an inner ring width of 40 Å.

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Proton transport coupled ATP synthesis by the purified yeast H+-ATP synthase in proteoliposomes

Biochimica et Biophysica Acta (BBA) - Bioenergetics ◽

10.1016/j.bbabio.2010.07.013 ◽

2010 ◽

Vol 1797 (11) ◽

pp. 1828-1837 ◽

Cited By ~ 20

Author(s):

Kathrin Förster ◽

Paola Turina ◽

Friedel Drepper ◽

Wolfgang Haehnel ◽

Susanne Fischer ◽

...

Keyword(s):

Atp Synthase ◽

Proton Transport ◽

Atp Synthesis

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Aerobic Growth of Escherichia coli Is Reduced, and ATP Synthesis Is Selectively Inhibited when Five C-terminal Residues Are Deleted from the ϵ Subunit of ATP Synthase

Journal of Biological Chemistry ◽

10.1074/jbc.m115.665059 ◽

2015 ◽

Vol 290 (34) ◽

pp. 21032-21041 ◽

Cited By ~ 20

Author(s):

Naman B. Shah ◽

Thomas M. Duncan

Keyword(s):

Escherichia Coli ◽

Atp Synthase ◽

Atp Hydrolysis ◽

Atp Synthesis ◽

Intrinsic Rate ◽

Synthesis Rate ◽

Final Segment ◽

Rotary Catalysis

F-type ATP synthases are rotary nanomotor enzymes involved in cellular energy metabolism in eukaryotes and eubacteria. The ATP synthase from Gram-positive and -negative model bacteria can be autoinhibited by the C-terminal domain of its ϵ subunit (ϵCTD), but the importance of ϵ inhibition in vivo is unclear. Functional rotation is thought to be blocked by insertion of the latter half of the ϵCTD into the central cavity of the catalytic complex (F1). In the inhibited state of the Escherichia coli enzyme, the final segment of ϵCTD is deeply buried but has few specific interactions with other subunits. This region of the ϵCTD is variable or absent in other bacteria that exhibit strong ϵ-inhibition in vitro. Here, genetically deleting the last five residues of the ϵCTD (ϵΔ5) caused a greater defect in respiratory growth than did the complete absence of the ϵCTD. Isolated membranes with ϵΔ5 generated proton-motive force by respiration as effectively as with wild-type ϵ but showed a nearly 3-fold decrease in ATP synthesis rate. In contrast, the ϵΔ5 truncation did not change the intrinsic rate of ATP hydrolysis with membranes. Further, the ϵΔ5 subunit retained high affinity for isolated F1 but reduced the maximal inhibition of F1-ATPase by ϵ from >90% to ∼20%. The results suggest that the ϵCTD has distinct regulatory interactions with F1 when rotary catalysis operates in opposite directions for the hydrolysis or synthesis of ATP.

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An ATP synthase harboring an atypical γ-subunit is involved in ATP synthesis in tomato fruit chromoplasts

The Plant Journal ◽

10.1111/tpj.12109 ◽

2013 ◽

Vol 74 (1) ◽

pp. 74-85 ◽

Cited By ~ 9

Author(s):

Irini Pateraki ◽

Marta Renato ◽

Joaquín Azcón-Bieto ◽

Albert Boronat

Keyword(s):

Atp Synthase ◽

Tomato Fruit ◽

Atp Synthesis ◽

Γ Subunit

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Purification and Biochemical Characterization of the F1Fo-ATP Synthase from Thermoalkaliphilic Bacillus sp. Strain TA2.A1

Journal of Bacteriology ◽

10.1128/jb.185.15.4442-4449.2003 ◽

2003 ◽

Vol 185 (15) ◽

pp. 4442-4449 ◽

Cited By ~ 45

Author(s):

Gregory M. Cook ◽

Stefanie Keis ◽

Hugh W. Morgan ◽

Christoph von Ballmoos ◽

Ulrich Matthey ◽

...

Keyword(s):

Atp Synthase ◽

Biochemical Characterization ◽

Atp Hydrolysis ◽

Sodium Dodecyl ◽

Electrical Potential ◽

Atp Synthesis ◽

Intrinsic Property ◽

Protein Sequencing ◽

Hydrolysis Activity

ABSTRACT We describe here purification and biochemical characterization of the F1Fo-ATP synthase from the thermoalkaliphilic organism Bacillus sp. strain TA2.A1. The purified enzyme produced the typical subunit pattern of an F1Fo-ATP synthase on a sodium dodecyl sulfate-polyacrylamide gel, with F1 subunits α, β, γ, δ, and ε and Fo subunits a, b, and c. The subunits were identified by N-terminal protein sequencing and mass spectroscopy. A notable feature of the ATP synthase from strain TA2.A1 was its specific blockage in ATP hydrolysis activity. ATPase activity was unmasked by using the detergent lauryldimethylamine oxide (LDAO), which activated ATP hydrolysis >15-fold. This activation was the same for either the F1Fo holoenzyme or the isolated F1 moiety, and therefore latent ATP hydrolysis activity is an intrinsic property of F1. After reconstitution into proteoliposomes, the enzyme catalyzed ATP synthesis driven by an artificially induced transmembrane electrical potential (Δψ). A transmembrane proton gradient or sodium ion gradient in the absence of Δψ was not sufficient to drive ATP synthesis. ATP synthesis was eliminated by the electrogenic protonophore carbonyl cyanide m-chlorophenylhydrazone, while the electroneutral Na+/H+ antiporter monensin had no effect. Neither ATP synthesis nor ATP hydrolysis was stimulated by Na+ ions, suggesting that protons are the coupling ions of the ATP synthase from strain TA2.A1, as documented previously for mesophilic alkaliphilic Bacillus species. The ATP synthase was specifically modified at its c subunits by N,N′-dicyclohexylcarbodiimide, and this modification inhibited ATP synthesis.

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