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Anti-Inflammatory Effect of Lactobacillus casei on Shigella-Infected Human Intestinal Epithelial Cells

Meng-Tsung Tien, Stephen E. Girardin, Béatrice Regnault, Lionel Le Bourhis, Marie-Agnès Dillies, Jean-Yves Coppée, Raphaëlle Bourdet-Sicard, Philippe J. Sansonetti and Thierry Pédron
J Immunol January 15, 2006, 176 (2) 1228-1237; DOI: https://doi.org/10.4049/jimmunol.176.2.1228
Meng-Tsung Tien
*Pathogénie Microbienne Moléculaire Unit, Institut National de la Santé et de la Recherche Médicale U389,
†DNA Chip Platform, Genopole, and
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Stephen E. Girardin
*Pathogénie Microbienne Moléculaire Unit, Institut National de la Santé et de la Recherche Médicale U389,
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Béatrice Regnault
†DNA Chip Platform, Genopole, and
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Lionel Le Bourhis
‡Imunité Innée et Signalisation, Pasteur Institute, Paris, France; and
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Marie-Agnès Dillies
†DNA Chip Platform, Genopole, and
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Jean-Yves Coppée
†DNA Chip Platform, Genopole, and
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Raphaëlle Bourdet-Sicard
§Danone Vitapole, Nutrivaleur, Palaiseau, France
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Philippe J. Sansonetti
*Pathogénie Microbienne Moléculaire Unit, Institut National de la Santé et de la Recherche Médicale U389,
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Thierry Pédron
*Pathogénie Microbienne Moléculaire Unit, Institut National de la Santé et de la Recherche Médicale U389,
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  •            FIGURE 1.
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    FIGURE 1.

    Hierarchical clustering modulated genes during infection of Caco-2 cells with Shigella, in the presence or absence of L. casei. Caco-2 cells were incubated overnight in the presence or absence of L. casei and challenged for 3 h with M90T-AfaE, the virulent strain of S. flexneri. Radioactive nucleotides were incorporated during cDNA synthesis. The labeled probes were hybridized onto macroarrays consisting of 1050 human genes represented by PCR products spotted onto nylon membranes. After washings and scanning, signal detection and normalization were performed allowing group comparisons. Modulated genes were then clustered using dChip software. Each row represents a gene, and each column represents the mean expression for each replicate. The red color represents an expression level above the mean expression of a gene across all samples, and the blue color represents an expression level lower than the mean. For each condition, eight biological replicates were made.

  •            FIGURE 2.
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    FIGURE 2.

    Anti-inflammatory effect of L. casei. The cells were treated as described in Material and Methods and in the legend to Fig. 1. After RNA extraction, cDNA was synthetized using Oligo-dT and reverse transcriptase enzyme. Five microliters of a 1/20 dilution were used as a template for the PCR. A, Confluent, polarized Caco-2 cells were used. B, Densitometric quantification of PCR products ((gene/GAPDH) × 100).

  •            FIGURE 3.
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    FIGURE 3.

    Inhibition of Shigella-induced NF-κB activation by L. casei. Overnight preincubation of HEK293 cells with L. casei blocks NF-κB activation induced by the invasive bacteria S. flexneri. CTR, Control.

  •            FIGURE 4.
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    FIGURE 4.

    L. casei infection results in up-regulation of I-κBα protein and inhibits Shigella-induced I-κBα degradation. A, Overnight preincubation of HEK293 cells with L. casei induces the up-regulation of I-κBα protein, while leaving other proteins of the Nod1-dependent signaling pathway unchanged. B, Overnight (O/N) preincubation of HEK293 cells with L. casei blocks I-κBα degradation induced by the invasive bacteria S. flexneri. CTR, Control.

  •            FIGURE 5.
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    FIGURE 5.

    L. casei infection results in up-regulation of the phosphorylated form of the I-κBα protein. Overnight (O/N) preincubation of HEK293 cells with L. casei (ranging from 2.5 106 to 5.107 bacteria/ml) induced a dose-dependent increase of I-κBα protein phosphorylation as determined by Western blotting using a specific polyclonal anti-human phospho-I-κBα Ab. CTR, Control.

  •            FIGURE 6.
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    FIGURE 6.

    Inhibition of TNF-α-induced NF-κB activation by L. casei. A, HEK293 cells were preincubated overnight with L. casei or MRS buffer (control medium) before stimulation for 4 h with TNF-α. Three bacterial concentrations were used: 5.106, 2.107, or 5.107 bacteria/ml. B, HEK293 cells were preincubated overnight with L. casei or MRS buffer (control medium) before stimulation for various times (15, 30, or 45 min) with TNF-α, followed by lysis of the cells. The I-κBα protein content was determined by Western blotting using a polyclonal anti-human I-κBα Ab. CTR, Control.

  •            FIGURE 7.
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    FIGURE 7.

    L. casei induced a down-regulation of genes involved in ubiquitination/degradation processes. Caco-2 cells were cultured overnight with L. casei with a MOI of 100. A, After washes with PBS and RNA extraction with the Rneasy mini kit, cDNA was synthetized using oligo-d(T) and reverse transcriptase. PCRs were performed as described in the legend to Fig. 2. B, After washes with PBS and lysis with Laemmli buffer, aliquots of the lysates were loaded on 15 or 10% SDS-PAGE for the subsequent detection of Rbx-1 or tubulin, respectively. The Rbx-1 or tubulin protein contents were determined by Western blotting using a polyclonal anti-human Rbx-1 or a monoclonal anti-human tubulin Ab, respectively. C, HEK cells were treated overnight with L. casei or for 6 h with 50 μM of the proteasome inhibitor MG-132 before incubation with or without TNF. The I-κBα protein content and global ubiquitinated proteins were determined by Western blotting (WB) using a polyclonal anti-human I-κBα Ab or monoclonal anti-ubiquitin Ab, respectively.

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    Table I.

    PCR primers used for PCRs

    Gene NameForwardReverseLength
    GAPDH TGAAGGTCGGAGTCAACGGATTTGGTCATGTGGGCCATGAGGTCCACCAC983
    Amphiregulin CTAGTAGTGAACCGTCCTCGCTCCTTCATATTTCCTGACG489
    CXCL1 TGTCAACCCCAAGTTAGTTCTCAATAATTAAGCCCCTTTG400
    CXCL2 CCAAAGTGTGAAGGTGAAGTATGGGAGAGTGTGCAAGTAG400
    IL-8 ATGACTTCCAAGCTGGCCGTGGCTTCTCAGCCCTCTTCAAAAACTTCTC289
    ICAM-1 AGTCACCTATGGCAACGACTCCGGCCATACAGGACACGAAGCT401
    Rbx-1 AAGAAGCGCTTTGAAGTGAAGGTAACAGCAGGGAAAGTCA339
    Skp-1 GGAAATTGCCAAACAATCTGTTGAAGGTCTTGCGAATCTC366
    Proteasome ATPase 1 CAATCATGCCATCGTGTCTAGAGCCAACCACTCTCAAGAA405
    Proteasome ATPase 6 CAGCTGGACTGCAATTTCTTGCGAACATACCTGCTTCAGT494
    • View popup
    Table II.

    Macroarray analysis of polarized Caco-2 cell gene expression during Shigella infectiona

    Probe SetNI (mean ± SD)M90T (mean ± SD)P valueFold Change
    Vimentin14.62 ± 0.1814.15 ± 0.130.041027−1.39
    Postmeiotic segregation 114.32 ± 0.0913.97 ± 0.090.008549−1.27
    Human chemokine α 3 (CKA-3)13.44 ± 0.113.1 ± 0.090.015804−1.27
    Collagen, type II, α 114.23 ± 0.1213.91 ± 0.090.038098−1.25
    PAC 179D313.8 ± 0.0813.55 ± 0.050.009966−1.20
    Uk-1313.59 ± 0.0513.39 ± 0.060.015796−1.16
    v-erb-a avian erythroblastic leukemia viral oncogene13.35 ± 0.0913.14 ± 0.030.045152−1.16
    Bullous pemphigoid antigen 113.25 ± 0.0613.05 ± 0.050.014533−1.15
    FK506-binding protein 1A (12 kDa)13.75 ± 0.0713.55 ± 0.060.043947−1.15
    Flavin containing monooxygenase 413.11 ± 0.0312.95 ± 0.040.004456−1.13
    FK506-binding protein 4 (59 kDa)13.36 ± 0.0613.19 ± 0.040.031667−1.12
    Bcl-2 binding protein13.35 ± 0.0513.2 ± 0.030.012662−1.11
    Heparan sulfate proteoglycan 213.15 ± 0.0513.02 ± 0.050.041943−1.10
    IL-213.09 ± 0.0913.32 ± 0.040.0236951.18
    CXCL113.09 ± 0.0813.33 ± 0.080.0421541.19
    IEX13.21 ± 0.0513.45 ± 0.080.0164121.19
    Connective tissue growth factor13.05 ± 0.0513.36 ± 0.070.0008671.24
    CXCL312.9 ± 0.0713.22 ± 0.120.0370181.24
    Coproporphyrinogen oxidase14.19 ± 0.0814.53 ± 0.10.012931.27
    SOCS-313.34 ± 0.1213.68 ± 0.10.0322771.27
    CL100 mRNA for protein tyrosine phosphatase12.9 ± 0.0713.24 ± 0.080.0032151.27
    IRF-112.99 ± 0.0613.37 ± 0.140.0198691.30
    Ribosomal protein S317.22 ± 0.1117.63 ± 0.090.0096221.32
    Ryudocan13.99 ± 0.0714.4 ± 0.140.021051.32
    MAD-3 (IK-B like activity)12.95 ± 0.0713.37 ± 0.130.0072911.34
    CCL20 (MIP-3 α)13.61 ± 0.1214.1 ± 0.180.0324251.39
    GRO-2 oncogene12.91 ± 0.113.42 ± 0.180.0188731.42
    Heat shock 70 KDa protein 614.09 ± 0.1214.61 ± 0.120.0055951.42
    Homo sapiens chemokine exodus-112.73 ± 0.113.27 ± 0.220.037421.45
    TNF ip2013.16 ± 0.0313.74 ± 0.140.0009841.49
    Amphiregulin13.92 ± 0.1614.52 ± 0.10.0034591.52
    CXCL213.37 ± 0.0614.01 ± 0.230.0153171.56
    EST-214.46 ± 0.215.11 ± 0.140.0110171.58
    v-jun13.4 ± 0.1214.14 ± 0.130.0003431.67
    Superoxide dismutase 2, mitochondrial16.83 ± 0.2517.66 ± 0.30.0411351.77
    Heat shock 70 KDa protein 1A15.12 ± 0.1816.28 ± 0.120.0000132.23
    • a Signal intensity resulting from macroarray hybridizations done with eight biological replicates of M90T infected Caco-2 cells were normalized and log2 transformed. Data analysis using the unpaired Welch t test from the dChip software gives a fold change between experimental point and baseline in a linear scale and an associated p value. Results with a p < 0.05 were considered as statistically significant.

    • View popup
    Table III.

    Determination of modulated probe sets during time course culture of Caco-2 cells with L. caseia

    Time CourseProbe Set Number
    DecreaseIncrease
    2 h5335
    6 h6359
    24 h357237
    • a Caco-2 cells were cultured 2, 6, or 24 h with L. casei. After RNA extraction, labeling and hybridizations onto U133A Affymetrix GeneChip were performed. The number represents the modulated probe set with a fold change > 2.

    • View popup
    Table IV.

    Gene expression modulation during L. casei time coursea

    GO Biological ProcessbProbe SetRefSeq IDGene NameModulationcFold Changed
    Group 1: Cell growth/cell cycle201278_atNM_001343Disabled homolog 2, mitogen-responsive phosphoprotein (Drosophila)D−4.68
    201202_atNM_002592Proliferating cell nuclear antigenD−4.29
    216237_s_atNM_006739MCM5 minichromosome maintenance deficient 5, cell division cycle 46D−4.07
    203625_x_atNM_005983S-phase kinase-associated protein 2 (p45)D−3.93
    204318_s_atNM_016426G-2 and S-phase expressed 1D−3.42
    204709_s_atNM_004856Kinesin family member 23D−3.14
    200659_s_atNM_002634ProhibitinD−3.08
    209662_atNM_004365Centrin, EF-hand protein, 3 (CDC3 1 homolog, yeast)D−2.98
    204162_atNM_006101Kinetochore associated 2D−2.88
    214710_s_atNM_031966Cyclin B1D−2.83
    207165_atNM_012484Hyaluronan-mediated motility receptor (RHAMM)D−2.73
    202883_s_atNM_002716Protein phosphatase 2 (formerly 2A), regulatory subunit A (PR 65), βD−2.73
    208712_atNM_001758Cyclin D1 (PRAD1: parathyroid adenomatosis 1)D−2.51
    213222_atNM_015192Phospholipase C, β 1 (phosphoinositide-specific)D−2.51
    203145_atNM_006461Sperm associated antigen 5D−2.46
    204444_atNM_004523Kinesin family member 11D−2.46
    202240_atNM_005030Polo-like kinase 1 (Drosophila)D−2.42
    200959_atNM_004960fusion (involved in t(12;16) in malignant liposarcoma)D−2.38
    218350_s_atNM_015895geminin, DNA replication inhibitorD−2.34
    203078_atNM_003591Cullin 2D−2.30
    203362_s_atNM_002358MAD2 mitotic arrest deficient-like 1 (yeast)D−2.22
    212426_s_atNM_006826Tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activationD−2.22
    212949_atNM_015341Barren homolog (Drosophila)D−2.18
    208727_s_atNM_001791cell division cycle 42 (GTP binding protein, 25 kDa)D−2.18
    201938_atNM_004642CDK2-associated protein 1D−2.14
    203740_atNM_005792M-phase phosphoprotein 6D−2.03
    201664_atNM_0012799SMC4 structural maintenance of chromosomes 4-like 1 (yeast)D−1.90
    218009_s_atNM_003981Protein regulator of cytokinesis 1D−1.90
    201725_atNM_006023Chromosome 10 open reading frame 7D−1.87
    220789_s_atNM_004749Transforming growth factor β regulator 4D−1.87
    204817_atNM_012291Extra spindle poles like 1 (S. cerevisiae)D−1.87
    201186_atNM_002337Low-density lipoprotein receptor-related protein associated protein 1D−1.65
    221509_atNM_003677Density-regulated proteinD−1.57
    201173_x_atNM_006600Nuclear distribution gene C homolog (A. nidulans)D−1.46
    217839_atNM_006070TRK-fused geneI1.87
    219910_atNM_007076Huntingtin interacting protein EI2.38
    203226_s_atNM_005981Sarcoma amplified sequenceI2.55
    202205_atNM_003370Vasodilator-stimulated phosphoproteinI3.86
    202061_s_atNM_005065sel-1 suppressor of lin-12-like (C. elegans)I3.86
    210513_s_atNM_003376Vascular endothelial growth factorI4.07
    205569_atNM_014398Lysosomal-associated membrane protein 3I4.92
    200598_s_atNM_003299Tumor rejection antigen (gp96) 1I5.46
    Group 2: Apoptosis220643_s_atNM_018147Fas apoptotic inhibitory moleculeD−5.10
    221690_s_atNM_017852NACHT, leucine rich repeat and PYD containing 2 (Nalp2)D−4.68
    202268_s_atNM_003905Amyloid β precursor protein binding protein 1, 59 KDaD−2.14
    220044_x_atNM_006107Cisplatin resistance-associated overexpressed proteinD−2.14
    208424_s_atNM_020313Cytokine induced apoptosis inhibitor 1D−2.11
    219275_atNM_004708Programmed cell death 5D−1.65
    203489_atNM_006427CD27-binding (Siva) proteinD−1.49
    221479_s_atNM_004331BCL2/adenovirus E1B 19 kDa interacting protein 3-likeI2.30
    202731_atNM_014456Programmed cell death 4 (neoplastic transformation inhibitor)I3.36
    202014_atNM_014330Protein phosphatase 1, regulatory (inhibitor) subunit 15AI7.21
    Group 3: Hypoxia200825_s_atNM_006389Hypoxia up-regulated 1I3.86
    202887_s_atNM_019058HIF-1 response RTP801I4.92
    Group 4: Ubiquitination/218117_atNM_014248Ring-box 1D−4.07
     degradation212751_atNM_003348Ubiquitin-conjugating enzyme E2N (UBC13 homolog, yeast)D−2.88
    201377_atNM_014847Ubiquitin associated protein 2-likeD−2.42
    201498_atNM_003470Ubiquitin specific protease 7 (herpes virus-associated)D−2.34
    211764_s_atNM_003338Ubiquitin-conjugating enzyme E2D 1 (UBC4/5 homolog, yeast)D−2.22
    • View popup
    Table IVA.

    Continued

    GO Biological ProcessbProbe SetRefSeq IDGene NameModulationcFold Changed
    201199_s_atNM_002807Proteasome (prosome, macropain) 26S subunit, non-ATPase, 1D−2.00
    204219_s_atNM_002802Proteasome (prosome, macropain) 26S subunit, ATPase, 1D−1.97
    200683_s_atNM_003347Ubiquitin-conjugating enzyme E2L 3D−1.93
    200988_s_atNM_005789Proteasome (prosome, macropain) activator subunit 3 (PA28 γ Ki)D−1.87
    201699_atNM_002806Proteasome (prosome, macropain) 26S subunit, ATPase, 6D−1.83
    202151_s_atNM_016172Ubiquitin associated domain containing 1D−1.77
    212987_atNM_012347F-box protein 9D−1.71
    202038_atNM_004788Ubiquitination factor E4A (UFD2 homolog, yeast)D−1.65
    202128_atNM_014821KIAA0317D−1.62
    200786_atNM_002799Proteasome (prosome, macropain) subunit, β type, 7D−1.57
    201671_x_atNM_005151Ubiquitin specific protease 14 (tRNA-guanine transglycosylase)D−1.46
    212576_atNM_015246Mahogunin, ring finger 1D−1.37
    208723_atNM_004651Ubiquitin specific protease 11D−1.21
    218582_atNM_017824Ring finger protein 153I1.74
    201133_s_atNM_014819Praja 2, RING-H2 motif containingI1.97
    208980_s_atNM_021009Ubiquitin CI2.07
    201881_s_atNM_005744Ariadne homolog, ubiquitin-conjugating enzyme E2 binding protein, 1I2.14
    221962_s_atNM_003344Ubiquitin-conjugating enzyme E2H (UBC8 homolog, yeast)I2.18
    208663_s_atNM_003316Tetratricopeptide repeat domain 3I2.34
    36564_atNM_153341BR domain containing 3I3.03
    • a The cells were treated as described in Table III⇑.

    • b Four different pathways were selected using the NetAffyx database.

    • c D and I indicate, respectively, whether the gene expression decreases or increases between the experimental point and the baseline (Caco-2 cells alone).

    • d Fold change between the experimental point and baseline in a linear scale.

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The Journal of Immunology: 176 (2)
The Journal of Immunology
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15 Jan 2006
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Anti-Inflammatory Effect of Lactobacillus casei on Shigella-Infected Human Intestinal Epithelial Cells
Meng-Tsung Tien, Stephen E. Girardin, Béatrice Regnault, Lionel Le Bourhis, Marie-Agnès Dillies, Jean-Yves Coppée, Raphaëlle Bourdet-Sicard, Philippe J. Sansonetti, Thierry Pédron
The Journal of Immunology January 15, 2006, 176 (2) 1228-1237; DOI: 10.4049/jimmunol.176.2.1228

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Anti-Inflammatory Effect of Lactobacillus casei on Shigella-Infected Human Intestinal Epithelial Cells
Meng-Tsung Tien, Stephen E. Girardin, Béatrice Regnault, Lionel Le Bourhis, Marie-Agnès Dillies, Jean-Yves Coppée, Raphaëlle Bourdet-Sicard, Philippe J. Sansonetti, Thierry Pédron
The Journal of Immunology January 15, 2006, 176 (2) 1228-1237; DOI: 10.4049/jimmunol.176.2.1228
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