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Current IssueEditorial BoardOnline First ArticlesArchive

Research Article

volume 54 issue 10 (october 2020) : 1285-1290,   Doi: 10.18805/ijar.B-1035

Caspase-11 plays an important role in IL-1, IL-18 and IL-1â secretion from porcine alveolar macrophage cells stimulated with Brucella suis LPS

H
Han-wei Jiao
Y
Yu Zhao
X
Xue-hong Shuai
L
Li Wu
B
Bo Liao
J
Ji-xuan Chen
Y
Yi-chen Luo
H
Hong-jun Wang
Q
Qing-zhou Huang
1College of Animal Science, Southwest University, Veterinary Scientific Engineering Research Center, College Road, RongChang 402460, ChongQing, People’s Republic of China.
Cite article:- Jiao Han-wei, Zhao Yu, Shuai Xue-hong, Wu Li, Liao Bo, Chen Ji-xuan, Luo Yi-chen, Wang Hong-jun, Huang Qing-zhou (2019). Caspase-11 plays an important role in IL-1, IL-18 and IL-1â secretion from porcine alveolar macrophage cells stimulated with Brucella suis LPS. Indian Journal of Animal Research. 54(10): 1285-1290. doi: 10.18805/ijar.B-1035.

ABSTRACT

Brucella spp. is the causative agent of brucellosis, an extremely important disease worldwide. Innate immune cells detect pathogens via repeated cellular patterns (PAMPs) such as the Brucella suis (B. suis) lipopolysaccharide (LPS) coat on Gram-negative bacteria, which act as an important virulence factor of Brucella. B.suis LPS may be an issue for pro-inflammatory cytokine induction such as interleukin-1 (IL-1), interleukin-18 (IL-18) and interleukin-1â (IL-1â), which released from immune cells to mediate downstream inflammatory effects. To elucidate the mechanism of how B.suis LPS affects the secretion of IL-1, IL-18 and IL-1â in macrophages. We identified the up-regulation of caspase-11 in a porcine alveolar macrophages (PAM) cells stimulated with B.suis LPS. Furthermore, specific small interfering RNA (siRNA) targeting caspase-11 effectively inhibited B.suis LPS stimulated IL-1, IL-18 and IL-1â release from PAM. The results indicated that the concentrations of IL-1, IL-18 and IL-1â of caspase-11 siRNA pretreated group were lower than that of control significantly. Caspase-11 plays an important role in IL-1, IL-18 and IL-1â secretion from porcine alveolar macrophage cells stimulated with Brucella suis LPS, and these findings might aid our understanding of the pathogenic mechanisms of Brucella and provide an entirely new innate immune response mechanism underlying macrophages dysfunction during Brucella infection.

REFERENCES

  1. Ahmed, W., Zheng, K., Liu, Z.F. (2016). Establishment of Chronic Infection: Brucella’s Stealth Strategy. Frontiers in Cellular and Infection Microbiology, 15: 6-30. 
  2. Amit-Kumar, V.K., Gupta, A.R., Rajesh M., Verma A.K., Yadav S.K. (2018). Nanoparticle based Brucella melitensis vaccine induced oxidative stress acts in synergism to immune response. Indian Journal Of Animal Research, DOI: 10.18805/ijar.B-3548. 
  3. Aparajita, D., Bablu, K., Soumendu, C., Karam, P.S., Garima, S. (2018). Single-tube duplex-PCR for specific detection and differentiation of Brucella abortus S19 vaccine strain from other Brucella spp. Indian Journal Of Animal Research, DOI: 10.18805/ijar.B-    3584. 
  4. Baldi, P.C., and Giambartolomei, G.H. (2013). Pathogenesis and pathobiology of zoonotic brucellosis in humans. Revue Scientifique Et Technique-Office International Des Epizooties, 32:117-125.
  5. Barquero-Calvo, E., Mora-Cartín, R., Arce-Gorvel, V., de-Diego, J.L., Chacón-Díaz, C., Chaves-Olarte, E., et al. (2015). Brucella abortus Induces the Premature Death of Human Neutrophils through the action of its Lipopolysaccharide. PLOS Pathogens, 11:e1004853.
  6. Billard, E., Dornand, J., Gross, A. (2007). Interaction of Brucella suis and Brucella abortus rough strains with human dendritic cells. Infection and Immunity, 75: 5916-5923. 
  7. Cardoso, P.G., Macedo, G.C., Azevedo, V., Oliveira, S.C. (2006). Brucella spp noncanonical LPS: structure, biosynthesis, and interaction with host immune system. Microbial Cell Factories, 23: 5-13.
  8. Cui, B., Liu, W., Wang, X., Chen, Y., Du, Q., Zhao, X., Zhang, H., Liu, S.L., Tong, D., Huang, Y. (2017). Brucella Omp25 Upregulates miR-155, miR-21-5p, and miR-23b to Inhibit Interleukin-12 Production via Modulation of Programmed Death-1 Signaling in Human Monocyte/Macrophages. Frontiers in Immunology, 8: 708. 
  9. Czibener, C., Del-Giudice, M.G., Spera, J.M., Fulgenzi, F.R., Ugalde, J.E. (2016). Delta-pgm, a new live-attenuated vaccine against Brucella suis. Vaccine, 34: 1524-1530. 
  10. Di, D.D., Jiang, H., Tian, L.L., Kang, J.L., Zhang, W., Yi, X.P., Ye, F., Zhong, Q., Ni, B., He, Y.Y., Xia, L., et al. (2016). Comparative genomic analysis between newly sequenced Brucella suis Vaccine Strain S2 and the Virulent Brucella suis Strain 1330. BMC Genomics, 17: 741.
  11. Dinarello, C.A. (2011). Interleukin-1 in the pathogenesis and treatment of inflammatory diseases. Blood, 117: 3720-3732. 
  12. Jakka, P., Namani, S., Murugan, S., Rai, N., Radhakrishnan, G. (2017). The Brucella effector protein TcpB induces degradation of inflammatory caspases and thereby subverts non-canonical inflammasome activation in macrophages. Journal of Biological Chemistry, 292: 20613-20627. 
  13. Jiao, H.W., Jia, X.X., Zhao, T.J., Rong, H., Zhang, J.N., Cheng, Y., Zhu, H.P., Xu, K.L., Guo, S.Y., et al. (2016). Up-regulation of TDAG51 is a dependent factor of LPS-induced RAW264.7 macrophages proliferation and cell cycle progression. Immunopharmacol    Immunotoxicol, 38: 124-130.
  14. Ke, Y., Wang, Y., Li, W., Chen, Z. (2015). Type IV secretion system of Brucella spp. and its effectors. Frontiers in Cellular and Infection Microbiology, 5: 72. 
  15. Lei, M., Du, L., Jiao, H., Cheng, Y., Zhang, D., Hao, Y., Li, G., Qiu, W., Fan, Q., Li, C., Chen, C., Wang, F. (2012). Inhibition of mCD14 inhibits TNFá secretion and NO production in RAW264.7 cells stimulated by Brucella melitensis infection. Veterinary Microbiology, 160: 362-368.
  16. Losa, R., Bablu, K., Ankita, J., Arockiasamy A.P. (2018). Acellular outer membrane vesicles of Brucella abortus strain 19 elicits both humoral and cell mediated immune response in mice. Indian Journal Of Animal Research, DOI: 10.18805/ijar.B-3428.
  17. Porte, F., Naroeni, A., Ouahrani-Bettache, S., Liautard, JP. (2003). Role of the Brucella suis lipopolysaccharide O antigen in phagosomal genesis and in inhibition of phagosome-lysosome fusion in murine macrophages. Infection and Immunity 71: 1481-1490.
  18. Roset, M.S., Almirón, M.A. (2013). FixL-like sensor FlbS of Brucella abortus binds haem and is necessary for survival within eukaryotic cells. FEBS Letter, 17: 3102-3107. 
  19. Sahoo, M., Ceballos-Olvera, I., del-Barrio, L., Re, F. (2011). Role of the inflammasome, IL-1â, and IL-18 in bacterial infections. Scientific World Journal, 11: 2037-2050.
  20. Tsai, C.M., Frasch, C.E. (1982). A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels. Analytical Biochemistry, 49: 45-49. 
  21. Zanoni, I., Tan, Y., Di, Gioia M., Broggi, A., Ruan, J., Shi, J., Donado, C.A., Shao, F., Wu, H., Springstead, J.R., Kagan, J.C.(2016). An endogenous caspase-11 ligand elicits interleukin-1 release from living dendritic cells. Science, 352: 1232-1236. 
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Indian Journal of Animal Research
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    Research Article

    volume 54 issue 10 (october 2020) : 1285-1290,   Doi: 10.18805/ijar.B-1035

    Caspase-11 plays an important role in IL-1, IL-18 and IL-1â secretion from porcine alveolar macrophage cells stimulated with Brucella suis LPS

    H
    Han-wei Jiao
    Y
    Yu Zhao
    X
    Xue-hong Shuai
    L
    Li Wu
    B
    Bo Liao
    J
    Ji-xuan Chen
    Y
    Yi-chen Luo
    H
    Hong-jun Wang
    Q
    Qing-zhou Huang
    1College of Animal Science, Southwest University, Veterinary Scientific Engineering Research Center, College Road, RongChang 402460, ChongQing, People’s Republic of China.
    Cite article:- Jiao Han-wei, Zhao Yu, Shuai Xue-hong, Wu Li, Liao Bo, Chen Ji-xuan, Luo Yi-chen, Wang Hong-jun, Huang Qing-zhou (2019). Caspase-11 plays an important role in IL-1, IL-18 and IL-1â secretion from porcine alveolar macrophage cells stimulated with Brucella suis LPS. Indian Journal of Animal Research. 54(10): 1285-1290. doi: 10.18805/ijar.B-1035.

    ABSTRACT

    Brucella spp. is the causative agent of brucellosis, an extremely important disease worldwide. Innate immune cells detect pathogens via repeated cellular patterns (PAMPs) such as the Brucella suis (B. suis) lipopolysaccharide (LPS) coat on Gram-negative bacteria, which act as an important virulence factor of Brucella. B.suis LPS may be an issue for pro-inflammatory cytokine induction such as interleukin-1 (IL-1), interleukin-18 (IL-18) and interleukin-1â (IL-1â), which released from immune cells to mediate downstream inflammatory effects. To elucidate the mechanism of how B.suis LPS affects the secretion of IL-1, IL-18 and IL-1â in macrophages. We identified the up-regulation of caspase-11 in a porcine alveolar macrophages (PAM) cells stimulated with B.suis LPS. Furthermore, specific small interfering RNA (siRNA) targeting caspase-11 effectively inhibited B.suis LPS stimulated IL-1, IL-18 and IL-1â release from PAM. The results indicated that the concentrations of IL-1, IL-18 and IL-1â of caspase-11 siRNA pretreated group were lower than that of control significantly. Caspase-11 plays an important role in IL-1, IL-18 and IL-1â secretion from porcine alveolar macrophage cells stimulated with Brucella suis LPS, and these findings might aid our understanding of the pathogenic mechanisms of Brucella and provide an entirely new innate immune response mechanism underlying macrophages dysfunction during Brucella infection.

    REFERENCES

    1. Ahmed, W., Zheng, K., Liu, Z.F. (2016). Establishment of Chronic Infection: Brucella’s Stealth Strategy. Frontiers in Cellular and Infection Microbiology, 15: 6-30. 
    2. Amit-Kumar, V.K., Gupta, A.R., Rajesh M., Verma A.K., Yadav S.K. (2018). Nanoparticle based Brucella melitensis vaccine induced oxidative stress acts in synergism to immune response. Indian Journal Of Animal Research, DOI: 10.18805/ijar.B-3548. 
    3. Aparajita, D., Bablu, K., Soumendu, C., Karam, P.S., Garima, S. (2018). Single-tube duplex-PCR for specific detection and differentiation of Brucella abortus S19 vaccine strain from other Brucella spp. Indian Journal Of Animal Research, DOI: 10.18805/ijar.B-    3584. 
    4. Baldi, P.C., and Giambartolomei, G.H. (2013). Pathogenesis and pathobiology of zoonotic brucellosis in humans. Revue Scientifique Et Technique-Office International Des Epizooties, 32:117-125.
    5. Barquero-Calvo, E., Mora-Cartín, R., Arce-Gorvel, V., de-Diego, J.L., Chacón-Díaz, C., Chaves-Olarte, E., et al. (2015). Brucella abortus Induces the Premature Death of Human Neutrophils through the action of its Lipopolysaccharide. PLOS Pathogens, 11:e1004853.
    6. Billard, E., Dornand, J., Gross, A. (2007). Interaction of Brucella suis and Brucella abortus rough strains with human dendritic cells. Infection and Immunity, 75: 5916-5923. 
    7. Cardoso, P.G., Macedo, G.C., Azevedo, V., Oliveira, S.C. (2006). Brucella spp noncanonical LPS: structure, biosynthesis, and interaction with host immune system. Microbial Cell Factories, 23: 5-13.
    8. Cui, B., Liu, W., Wang, X., Chen, Y., Du, Q., Zhao, X., Zhang, H., Liu, S.L., Tong, D., Huang, Y. (2017). Brucella Omp25 Upregulates miR-155, miR-21-5p, and miR-23b to Inhibit Interleukin-12 Production via Modulation of Programmed Death-1 Signaling in Human Monocyte/Macrophages. Frontiers in Immunology, 8: 708. 
    9. Czibener, C., Del-Giudice, M.G., Spera, J.M., Fulgenzi, F.R., Ugalde, J.E. (2016). Delta-pgm, a new live-attenuated vaccine against Brucella suis. Vaccine, 34: 1524-1530. 
    10. Di, D.D., Jiang, H., Tian, L.L., Kang, J.L., Zhang, W., Yi, X.P., Ye, F., Zhong, Q., Ni, B., He, Y.Y., Xia, L., et al. (2016). Comparative genomic analysis between newly sequenced Brucella suis Vaccine Strain S2 and the Virulent Brucella suis Strain 1330. BMC Genomics, 17: 741.
    11. Dinarello, C.A. (2011). Interleukin-1 in the pathogenesis and treatment of inflammatory diseases. Blood, 117: 3720-3732. 
    12. Jakka, P., Namani, S., Murugan, S., Rai, N., Radhakrishnan, G. (2017). The Brucella effector protein TcpB induces degradation of inflammatory caspases and thereby subverts non-canonical inflammasome activation in macrophages. Journal of Biological Chemistry, 292: 20613-20627. 
    13. Jiao, H.W., Jia, X.X., Zhao, T.J., Rong, H., Zhang, J.N., Cheng, Y., Zhu, H.P., Xu, K.L., Guo, S.Y., et al. (2016). Up-regulation of TDAG51 is a dependent factor of LPS-induced RAW264.7 macrophages proliferation and cell cycle progression. Immunopharmacol    Immunotoxicol, 38: 124-130.
    14. Ke, Y., Wang, Y., Li, W., Chen, Z. (2015). Type IV secretion system of Brucella spp. and its effectors. Frontiers in Cellular and Infection Microbiology, 5: 72. 
    15. Lei, M., Du, L., Jiao, H., Cheng, Y., Zhang, D., Hao, Y., Li, G., Qiu, W., Fan, Q., Li, C., Chen, C., Wang, F. (2012). Inhibition of mCD14 inhibits TNFá secretion and NO production in RAW264.7 cells stimulated by Brucella melitensis infection. Veterinary Microbiology, 160: 362-368.
    16. Losa, R., Bablu, K., Ankita, J., Arockiasamy A.P. (2018). Acellular outer membrane vesicles of Brucella abortus strain 19 elicits both humoral and cell mediated immune response in mice. Indian Journal Of Animal Research, DOI: 10.18805/ijar.B-3428.
    17. Porte, F., Naroeni, A., Ouahrani-Bettache, S., Liautard, JP. (2003). Role of the Brucella suis lipopolysaccharide O antigen in phagosomal genesis and in inhibition of phagosome-lysosome fusion in murine macrophages. Infection and Immunity 71: 1481-1490.
    18. Roset, M.S., Almirón, M.A. (2013). FixL-like sensor FlbS of Brucella abortus binds haem and is necessary for survival within eukaryotic cells. FEBS Letter, 17: 3102-3107. 
    19. Sahoo, M., Ceballos-Olvera, I., del-Barrio, L., Re, F. (2011). Role of the inflammasome, IL-1â, and IL-18 in bacterial infections. Scientific World Journal, 11: 2037-2050.
    20. Tsai, C.M., Frasch, C.E. (1982). A sensitive silver stain for detecting lipopolysaccharides in polyacrylamide gels. Analytical Biochemistry, 49: 45-49. 
    21. Zanoni, I., Tan, Y., Di, Gioia M., Broggi, A., Ruan, J., Shi, J., Donado, C.A., Shao, F., Wu, H., Springstead, J.R., Kagan, J.C.(2016). An endogenous caspase-11 ligand elicits interleukin-1 release from living dendritic cells. Science, 352: 1232-1236. 
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