The Shigella flexneri virulence factor apyrase is released inside eukaryotic cells to hijack host cell fate

Intestinal epithelial cells represent the first line of defense from invading enteric pathogens. During the course of infection, pro-inflammatory programmed cell death is an effective way to eliminate invading microbes and to create a localized inflammatory environment. On the other hand, pathogens...

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Published inMicrobiology spectrum Vol. 11; no. 6; p. e0077523
Main Authors Perruzza, Lisa, Zagaglia, Carlo, Vitiello, Laura, Sarshar, Meysam, Strati, Francesco, Pasqua, Martina, Grassi, Fabio, Nicoletti, Mauro, Palamara, Anna Teresa, Ambrosi, Cecilia, Scribano, Daniela
Format Journal Article
LanguageEnglish
Published United States American Society for Microbiology 12.12.2023
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Abstract Intestinal epithelial cells represent the first line of defense from invading enteric pathogens. During the course of infection, pro-inflammatory programmed cell death is an effective way to eliminate invading microbes and to create a localized inflammatory environment. On the other hand, pathogens evolved countless strategies to overcome cell death and to keep the host alive ensuring their spread. It was previously shown that Shigella flexneri apyrase interacts with OmpA to contribute to a proper polar exposition of IcsA, which mediates actin-based motility. However, apyrase is also an ATP-diphosphohydrolase whose catalytic activity function has not been elucidated yet. Herein, we demonstrated that apyrase contributes to the manipulation of host cell fate by S. flexneri since it is released within the host cell cytoplasm during infection to degrade intracellular ATP. Thus, apyrase contributes to prevent caspase-1 activation, thereby downregulating the activation of pyroptosis in infected cells. Overall, apyrase is involved in the modulation of host cell survival and dampens the inflammatory response. In this paper, we demonstrated that apyrase is released within the host cell cytoplasm during infection to target the intracellular ATP pool. By degrading intracellular ATP, apyrase contributes to prevent caspases activation, thereby inhibiting the activation of pyroptosis in infected cells. Our results show, for the first time, that apyrase is involved in the modulation of host cell survival, thereby aiding this pathogen to dampen the inflammatory response. This work adds a further piece to the puzzle of Shigella pathogenesis. Due to its increased spread worldwide, prevention and controlling strategies are urgently needed. Overall, this study highlighted apyrase as a suitable target for an anti-virulence therapy to tackle this pathogen.
AbstractList In this paper, we demonstrated that apyrase is released within the host cell cytoplasm during infection to target the intracellular ATP pool. By degrading intracellular ATP, apyrase contributes to prevent caspases activation, thereby inhibiting the activation of pyroptosis in infected cells. Our results show, for the first time, that apyrase is involved in the modulation of host cell survival, thereby aiding this pathogen to dampen the inflammatory response. This work adds a further piece to the puzzle of Shigella pathogenesis. Due to its increased spread worldwide, prevention and controlling strategies are urgently needed. Overall, this study highlighted apyrase as a suitable target for an anti-virulence therapy to tackle this pathogen.IMPORTANCEIn this paper, we demonstrated that apyrase is released within the host cell cytoplasm during infection to target the intracellular ATP pool. By degrading intracellular ATP, apyrase contributes to prevent caspases activation, thereby inhibiting the activation of pyroptosis in infected cells. Our results show, for the first time, that apyrase is involved in the modulation of host cell survival, thereby aiding this pathogen to dampen the inflammatory response. This work adds a further piece to the puzzle of Shigella pathogenesis. Due to its increased spread worldwide, prevention and controlling strategies are urgently needed. Overall, this study highlighted apyrase as a suitable target for an anti-virulence therapy to tackle this pathogen.
Intestinal epithelial cells represent the first line of defense from invading enteric pathogens. During the course of infection, pro-inflammatory programmed cell death is an effective way to eliminate invading microbes and to create a localized inflammatory environment. On the other hand, pathogens evolved countless strategies to overcome cell death and to keep the host alive ensuring their spread. It was previously shown that Shigella flexneri apyrase interacts with OmpA to contribute to a proper polar exposition of IcsA, which mediates actin-based motility. However, apyrase is also an ATP-diphosphohydrolase whose catalytic activity function has not been elucidated yet. Herein, we demonstrated that apyrase contributes to the manipulation of host cell fate by S. flexneri since it is released within the host cell cytoplasm during infection to degrade intracellular ATP. Thus, apyrase contributes to prevent caspase-1 activation, thereby downregulating the activation of pyroptosis in infected cells. Overall, apyrase is involved in the modulation of host cell survival and dampens the inflammatory response. IMPORTANCE In this paper, we demonstrated that apyrase is released within the host cell cytoplasm during infection to target the intracellular ATP pool. By degrading intracellular ATP, apyrase contributes to prevent caspases activation, thereby inhibiting the activation of pyroptosis in infected cells. Our results show, for the first time, that apyrase is involved in the modulation of host cell survival, thereby aiding this pathogen to dampen the inflammatory response. This work adds a further piece to the puzzle of Shigella pathogenesis. Due to its increased spread worldwide, prevention and controlling strategies are urgently needed. Overall, this study highlighted apyrase as a suitable target for an anti-virulence therapy to tackle this pathogen.
Intestinal epithelial cells represent the first line of defense from invading enteric pathogens. During the course of infection, pro-inflammatory programmed cell death is an effective way to eliminate invading microbes and to create a localized inflammatory environment. On the other hand, pathogens evolved countless strategies to overcome cell death and to keep the host alive ensuring their spread. It was previously shown that Shigella flexneri apyrase interacts with OmpA to contribute to a proper polar exposition of IcsA, which mediates actin-based motility. However, apyrase is also an ATP-diphosphohydrolase whose catalytic activity function has not been elucidated yet. Herein, we demonstrated that apyrase contributes to the manipulation of host cell fate by S. flexneri since it is released within the host cell cytoplasm during infection to degrade intracellular ATP. Thus, apyrase contributes to prevent caspase-1 activation, thereby downregulating the activation of pyroptosis in infected cells. Overall, apyrase is involved in the modulation of host cell survival and dampens the inflammatory response.
ABSTRACT Intestinal epithelial cells represent the first line of defense from invading enteric pathogens. During the course of infection, pro-inflammatory programmed cell death is an effective way to eliminate invading microbes and to create a localized inflammatory environment. On the other hand, pathogens evolved countless strategies to overcome cell death and to keep the host alive ensuring their spread. It was previously shown that Shigella flexneri apyrase interacts with OmpA to contribute to a proper polar exposition of IcsA, which mediates actin-based motility. However, apyrase is also an ATP-diphosphohydrolase whose catalytic activity function has not been elucidated yet. Herein, we demonstrated that apyrase contributes to the manipulation of host cell fate by S. flexneri since it is released within the host cell cytoplasm during infection to degrade intracellular ATP. Thus, apyrase contributes to prevent caspase-1 activation, thereby downregulating the activation of pyroptosis in infected cells. Overall, apyrase is involved in the modulation of host cell survival and dampens the inflammatory response. IMPORTANCE In this paper, we demonstrated that apyrase is released within the host cell cytoplasm during infection to target the intracellular ATP pool. By degrading intracellular ATP, apyrase contributes to prevent caspases activation, thereby inhibiting the activation of pyroptosis in infected cells. Our results show, for the first time, that apyrase is involved in the modulation of host cell survival, thereby aiding this pathogen to dampen the inflammatory response. This work adds a further piece to the puzzle of Shigella pathogenesis. Due to its increased spread worldwide, prevention and controlling strategies are urgently needed. Overall, this study highlighted apyrase as a suitable target for an anti-virulence therapy to tackle this pathogen.
Intestinal epithelial cells represent the first line of defense from invading enteric pathogens. During the course of infection, pro-inflammatory programmed cell death is an effective way to eliminate invading microbes and to create a localized inflammatory environment. On the other hand, pathogens evolved countless strategies to overcome cell death and to keep the host alive ensuring their spread. It was previously shown that Shigella flexneri apyrase interacts with OmpA to contribute to a proper polar exposition of IcsA, which mediates actin-based motility. However, apyrase is also an ATP-diphosphohydrolase whose catalytic activity function has not been elucidated yet. Herein, we demonstrated that apyrase contributes to the manipulation of host cell fate by S. flexneri since it is released within the host cell cytoplasm during infection to degrade intracellular ATP. Thus, apyrase contributes to prevent caspase-1 activation, thereby downregulating the activation of pyroptosis in infected cells. Overall, apyrase is involved in the modulation of host cell survival and dampens the inflammatory response. In this paper, we demonstrated that apyrase is released within the host cell cytoplasm during infection to target the intracellular ATP pool. By degrading intracellular ATP, apyrase contributes to prevent caspases activation, thereby inhibiting the activation of pyroptosis in infected cells. Our results show, for the first time, that apyrase is involved in the modulation of host cell survival, thereby aiding this pathogen to dampen the inflammatory response. This work adds a further piece to the puzzle of Shigella pathogenesis. Due to its increased spread worldwide, prevention and controlling strategies are urgently needed. Overall, this study highlighted apyrase as a suitable target for an anti-virulence therapy to tackle this pathogen.
In this paper, we demonstrated that apyrase is released within the host cell cytoplasm during infection to target the intracellular ATP pool. By degrading intracellular ATP, apyrase contributes to prevent caspases activation, thereby inhibiting the activation of pyroptosis in infected cells. Our results show, for the first time, that apyrase is involved in the modulation of host cell survival, thereby aiding this pathogen to dampen the inflammatory response. This work adds a further piece to the puzzle of pathogenesis. Due to its increased spread worldwide, prevention and controlling strategies are urgently needed. Overall, this study highlighted apyrase as a suitable target for an anti-virulence therapy to tackle this pathogen.
Author Grassi, Fabio
Palamara, Anna Teresa
Pasqua, Martina
Vitiello, Laura
Scribano, Daniela
Zagaglia, Carlo
Strati, Francesco
Perruzza, Lisa
Sarshar, Meysam
Nicoletti, Mauro
Ambrosi, Cecilia
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Cites_doi 10.1016/j.mib.2020.07.007
10.1128/JB.188.4.1620-1627.2006
10.1111/imr.12287
10.1016/j.ijmm.2017.03.002
10.3389/fcimb.2016.00038
10.1152/ajpgi.00137.2005
10.1111/j.1365-2958.1995.tb02301.x
10.1128/mSystems.00604-20
10.1371/journal.pone.0090230
10.1016/j.micinf.2012.05.009
10.1016/j.micinf.2019.02.001
10.1128/jb.178.6.1770-1773.1996
10.1007/s000180050212
10.1128/microbiolspec.BAI-0023-2019
10.1242/dmm.049414
10.1016/j.immuni.2013.11.013
10.1038/ncb1021
10.1038/cddis.2014.70
10.1128/iai.00614-21
10.1016/j.chom.2021.08.010
10.1038/s41586-021-04020-1
10.1016/j.chom.2011.05.005
10.1177/039463200802100325
10.1128/IAI.01011-10
10.1038/sj.cdd.4401661
10.1128/IAI.06245-11
10.1016/j.immuni.2015.10.009
10.1016/j.immuni.2017.03.016
10.3390/ijms19010199
10.1371/journal.pone.0049625
10.1128/CMR.00032-07
10.3390/ijms21155590
10.1111/j.1600-065X.2011.01044.x
10.1093/pcp/pcs119
10.1016/S0140-6736(17)33296-8
10.1371/journal.pone.0056834
10.3389/fcimb.2016.00028
10.1073/pnas.1406694111
10.1016/j.ijmm.2014.11.004
10.1016/j.bbrep.2016.08.010
10.1128/mBio.01520-19
10.1016/j.micres.2017.09.001
10.3390/microorganisms9020369
10.3389/fmolb.2016.00061
10.1093/femspd/ftab052
10.1038/s41392-021-00507-5
10.1099/00221287-148-8-2519
10.5455/aim.2012.20.167-173
10.1038/nature13683
10.1371/journal.pone.0070514
10.1111/1462-2920.15138
10.1111/j.1462-5822.2007.01089.x
10.7554/eLife.59022
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Issue 6
Keywords pyroptosis
Shigella flexneri
apyrase
host cell survival
inflammation
ATP
Language English
License This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license. https://creativecommons.org/licenses/by/4.0
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Cecilia Ambrosi and Daniela Scribano contributed equally to this article.
The authors declare no conflict of interest.
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References e_1_3_3_50_2
e_1_3_3_16_2
e_1_3_3_18_2
e_1_3_3_39_2
e_1_3_3_12_2
e_1_3_3_37_2
e_1_3_3_14_2
e_1_3_3_35_2
e_1_3_3_33_2
e_1_3_3_54_2
e_1_3_3_10_2
e_1_3_3_31_2
e_1_3_3_52_2
e_1_3_3_40_2
e_1_3_3_5_2
e_1_3_3_7_2
e_1_3_3_9_2
e_1_3_3_27_2
e_1_3_3_29_2
e_1_3_3_23_2
e_1_3_3_48_2
e_1_3_3_25_2
e_1_3_3_46_2
e_1_3_3_44_2
e_1_3_3_3_2
e_1_3_3_21_2
e_1_3_3_42_2
e_1_3_3_51_2
e_1_3_3_17_2
e_1_3_3_19_2
e_1_3_3_38_2
e_1_3_3_13_2
e_1_3_3_36_2
e_1_3_3_15_2
e_1_3_3_34_2
e_1_3_3_32_2
e_1_3_3_11_2
e_1_3_3_30_2
e_1_3_3_53_2
e_1_3_3_6_2
e_1_3_3_8_2
e_1_3_3_28_2
e_1_3_3_49_2
e_1_3_3_24_2
e_1_3_3_47_2
e_1_3_3_26_2
e_1_3_3_45_2
e_1_3_3_2_2
e_1_3_3_20_2
e_1_3_3_43_2
e_1_3_3_4_2
e_1_3_3_22_2
e_1_3_3_41_2
Brokatzky, D, Mostowy, S (B17) 2022; 15
Jorgensen, I, Miao, EA (B29) 2015; 265
Scribano, D, Damico, R, Ambrosi, C, Superti, F, Marazzato, M, Conte, MP, Longhi, C, Palamara, AT, Zagaglia, C, Nicoletti, M (B12) 2016; 8
Romero, S, Grompone, G, Carayol, N, Mounier, J, Guadagnini, S, Prevost, M-C, Sansonetti, PJ, Van Nhieu, GT (B41) 2011; 9
Scribano, D, Petrucca, A, Pompili, M, Ambrosi, C, Bruni, E, Zagaglia, C, Prosseda, G, Nencioni, L, Casalino, M, Polticelli, F, Nicoletti, M (B11) 2014; 9
Puhar, A, Tronchère, H, Payrastre, B, Nhieu, GTV, Sansonetti, PJ (B42) 2013; 39
Ambrosi, C, Sarshar, M, Aprea, MR, Pompilio, A, Di Bonaventura, G, Strati, F, Pronio, A, Nicoletti, M, Zagaglia, C, Palamara, AT, Scribano, D (B3) 2019; 21
Miao, EA, Rajan, JV, Aderem, A (B28) 2011; 243
Spari, D, Beldi, G (B44) 2020; 21
Yilmaz, O, Yao, L, Maeda, K, Rose, TM, Lewis, EL, Duman, M, Lamont, RJ, Ojcius, DM (B37) 2008; 10
Campbell-Valois, FX, Pontier, SM (B53) 2016; 6
Yang, D, He, Y, Muñoz-Planillo, R, Liu, Q, Núñez, G (B47) 2015; 43
Coutinho-Silva, R, Ojcius, DM (B39) 2012; 14
Ashida, H, Suzuki, T, Sasakawa, C (B22) 2021; 59
Yu, H, Rao, X, Zhang, K (B40) 2017; 205
Di Martino, ML, Falconi, M, Micheli, G, Colonna, B, Prosseda, G (B9) 2016; 3
Pasqua, M, Zennaro, A, Trirocco, R, Fanelli, G, Micheli, G, Grossi, M, Colonna, B, Prosseda, G (B25) 2021; 9
Wanford, JJ, Hachani, A, Odendall, C (B14) 2022; 90
Yu, P, Zhang, X, Liu, N, Tang, L, Peng, C, Chen, X (B16) 2021; 6
Rauch, I, Deets, KA, Ji, DX, von Moltke, J, Tenthorey, JL, Lee, AY, Philip, NH, Ayres, JS, Brodsky, IE, Gronert, K, Vance, RE (B49) 2017; 46
Udaondo, Z, Duque, E, Daddaoua, A, Caselles, C, Roca, A, Pizarro-Tobias, P, Ramos, JL (B33) 2020; 22
Puri, RV, Reddy, PV, Tyagi, AK (B34) 2013; 8
Killackey, SA, Sorbara, MT, Girardin, SE (B1) 2016; 6
Lee, JS, Yilmaz, Ö (B21) 2018; 19
Schnupf, P, Sansonetti, PJ (B6) 2019; 7
Santapaola, D, Casalino, M, Petrucca, A, Presutti, C, Zagaglia, C, Berlutti, F, Colonna, B, Nicoletti, M (B7) 2002; 148
Kentner, D, Martano, G, Callon, M, Chiquet, P, Brodmann, M, Burton, O, Wahlander, A, Nanni, P, Delmotte, N, Grossmann, J, Limenitakis, J, Schlapbach, R, Kiefer, P, Vorholt, JA, Hiller, S, Bumann, D (B43) 2014; 111
Mitchell, PS, Roncaioli, JL, Turcotte, EA, Goers, L, Chavez, RA, Lee, AY, Lesser, CF, Rauch, I, Vance, RE (B48) 2020; 9
Shi, J, Zhao, Y, Wang, Y, Gao, W, Ding, J, Li, P, Hu, L, Shao, F (B46) 2014; 514
Köseoğlu, VK, Agaisse, H (B52) 2019; 10
Rossolini, GM, Schippa, S, Riccio, ML, Berlutti, F, Macaskie, LE, Thaller, MC (B31) 1998; 54
Schroeder, GN, Hilbi, H (B5) 2008; 21
Li, Z, Liu, W, Fu, J, Cheng, S, Xu, Y, Wang, Z, Liu, X, Shi, X, Liu, Y, Qi, X, Liu, X, Ding, J, Shao, F (B50) 2021; 599
Crane, JK, Naeher, TM, Choudhari, SS, Giroux, EM (B19) 2005; 289
Mohapatra, NP, Soni, S, Rajaram, MVS, Strandberg, KL, Gunn, JS (B35) 2013; 8
Ambrosi, C, Pompili, M, Scribano, D, Zagaglia, C, Ripa, S, Nicoletti, M (B24) 2012; 7
Loterio, RK, Zamboni, DS, Newton, HJ (B30) 2021; 79
Parsot, C, Ménard, R, Gounon, P, Sansonetti, PJ (B26) 1995; 16
Santapaola, D, Del Chierico, F, Petrucca, A, Uzzau, S, Casalino, M, Colonna, B, Sessa, R, Berlutti, F, Nicoletti, M (B13) 2006; 188
Cauwels, A, Rogge, E, Vandendriessche, B, Shiva, S, Brouckaert, P (B20) 2014; 5
Leuzzi, A, Grossi, M, Di Martino, ML, Pasqua, M, Micheli, G, Colonna, B, Prosseda, G (B23) 2017; 307
Hatsugai, N, Perez Koldenkova, V, Imamura, H, Noji, H, Nagai, T (B45) 2012; 53
Dai, S, Mohapatra, NP, Schlesinger, LS, Gunn, JS (B38) 2012; 80
Kotloff, KL, Riddle, MS, Platts-Mills, JA, Pavlinac, P, Zaidi, AKM (B4) 2018; 391
Nicoletti, M, Santino, I, Petrucca, A, Del Chierico, F, Cannavacciuolo, S, Casalino, M, Sessa, R, Cipriani, P (B8) 2008; 21
Hill, J, Samuel, JE (B36) 2011; 79
Zamaraeva, MV, Sabirov, RZ, Maeno, E, Ando-Akatsuka, Y, Bessonova, SV, Okada, Y (B15) 2005; 12
Ambrosi, C, Scribano, D, Sarshar, M, Zagaglia, C, Singer, BB, Palamara, AT, Langelier, C (B2) 2020; 5
U Gandhi, N, B Chandra, S (B32) 2012; 20
Lazar, SW, Kolter, R (B27) 1996; 178
Ambrosi, C, Pompili, M, Scribano, D, Limongi, D, Petrucca, A, Cannavacciuolo, S, Schippa, S, Zagaglia, C, Grossi, M, Nicoletti, M (B10) 2015; 305
Tran Van Nhieu, G, Clair, C, Bruzzone, R, Mesnil, M, Sansonetti, P, Combettes, L (B18) 2003; 5
Luchetti, G, Roncaioli, JL, Chavez, RA, Schubert, AF, Kofoed, EM, Reja, R, Cheung, TK, Liang, Y, Webster, JD, Lehoux, I, Skippington, E, Reeder, J, Haley, B, Tan, MW, Rose, CM, Newton, K, Kayagaki, N, Vance, RE, Dixit, VM (B51) 2021; 29
References_xml – ident: e_1_3_3_23_2
  doi: 10.1016/j.mib.2020.07.007
– ident: e_1_3_3_14_2
  doi: 10.1128/JB.188.4.1620-1627.2006
– ident: e_1_3_3_30_2
  doi: 10.1111/imr.12287
– ident: e_1_3_3_24_2
  doi: 10.1016/j.ijmm.2017.03.002
– ident: e_1_3_3_2_2
  doi: 10.3389/fcimb.2016.00038
– ident: e_1_3_3_20_2
  doi: 10.1152/ajpgi.00137.2005
– ident: e_1_3_3_27_2
  doi: 10.1111/j.1365-2958.1995.tb02301.x
– ident: e_1_3_3_3_2
  doi: 10.1128/mSystems.00604-20
– ident: e_1_3_3_12_2
  doi: 10.1371/journal.pone.0090230
– ident: e_1_3_3_40_2
  doi: 10.1016/j.micinf.2012.05.009
– ident: e_1_3_3_4_2
  doi: 10.1016/j.micinf.2019.02.001
– ident: e_1_3_3_28_2
  doi: 10.1128/jb.178.6.1770-1773.1996
– ident: e_1_3_3_32_2
  doi: 10.1007/s000180050212
– ident: e_1_3_3_7_2
  doi: 10.1128/microbiolspec.BAI-0023-2019
– ident: e_1_3_3_18_2
  doi: 10.1242/dmm.049414
– ident: e_1_3_3_43_2
  doi: 10.1016/j.immuni.2013.11.013
– ident: e_1_3_3_19_2
  doi: 10.1038/ncb1021
– ident: e_1_3_3_21_2
  doi: 10.1038/cddis.2014.70
– ident: e_1_3_3_15_2
  doi: 10.1128/iai.00614-21
– ident: e_1_3_3_52_2
  doi: 10.1016/j.chom.2021.08.010
– ident: e_1_3_3_51_2
  doi: 10.1038/s41586-021-04020-1
– ident: e_1_3_3_42_2
  doi: 10.1016/j.chom.2011.05.005
– ident: e_1_3_3_9_2
  doi: 10.1177/039463200802100325
– ident: e_1_3_3_37_2
  doi: 10.1128/IAI.01011-10
– ident: e_1_3_3_16_2
  doi: 10.1038/sj.cdd.4401661
– ident: e_1_3_3_39_2
  doi: 10.1128/IAI.06245-11
– ident: e_1_3_3_48_2
  doi: 10.1016/j.immuni.2015.10.009
– ident: e_1_3_3_50_2
  doi: 10.1016/j.immuni.2017.03.016
– ident: e_1_3_3_22_2
  doi: 10.3390/ijms19010199
– ident: e_1_3_3_25_2
  doi: 10.1371/journal.pone.0049625
– ident: e_1_3_3_6_2
  doi: 10.1128/CMR.00032-07
– ident: e_1_3_3_45_2
  doi: 10.3390/ijms21155590
– ident: e_1_3_3_29_2
  doi: 10.1111/j.1600-065X.2011.01044.x
– ident: e_1_3_3_46_2
  doi: 10.1093/pcp/pcs119
– ident: e_1_3_3_5_2
  doi: 10.1016/S0140-6736(17)33296-8
– ident: e_1_3_3_36_2
  doi: 10.1371/journal.pone.0056834
– ident: e_1_3_3_54_2
  doi: 10.3389/fcimb.2016.00028
– ident: e_1_3_3_44_2
  doi: 10.1073/pnas.1406694111
– ident: e_1_3_3_11_2
  doi: 10.1016/j.ijmm.2014.11.004
– ident: e_1_3_3_13_2
  doi: 10.1016/j.bbrep.2016.08.010
– ident: e_1_3_3_53_2
  doi: 10.1128/mBio.01520-19
– ident: e_1_3_3_41_2
  doi: 10.1016/j.micres.2017.09.001
– ident: e_1_3_3_26_2
  doi: 10.3390/microorganisms9020369
– ident: e_1_3_3_10_2
  doi: 10.3389/fmolb.2016.00061
– ident: e_1_3_3_31_2
  doi: 10.1093/femspd/ftab052
– ident: e_1_3_3_17_2
  doi: 10.1038/s41392-021-00507-5
– ident: e_1_3_3_8_2
  doi: 10.1099/00221287-148-8-2519
– ident: e_1_3_3_33_2
  doi: 10.5455/aim.2012.20.167-173
– ident: e_1_3_3_47_2
  doi: 10.1038/nature13683
– ident: e_1_3_3_35_2
  doi: 10.1371/journal.pone.0070514
– ident: e_1_3_3_34_2
  doi: 10.1111/1462-2920.15138
– ident: e_1_3_3_38_2
  doi: 10.1111/j.1462-5822.2007.01089.x
– ident: e_1_3_3_49_2
  doi: 10.7554/eLife.59022
– volume: 20
  start-page: 167
  year: 2012
  end-page: 173
  ident: B32
  article-title: A comparative analysis of three classes of bacterial non-specific acid phosphatases and archaeal phosphoesterases: evolutionary perspective
  publication-title: Acta Inform Med
  doi: 10.5455/aim.2012.20.167-173
– volume: 8
  year: 2013
  ident: B34
  article-title: Secreted acid phosphatase (SapM) of Mycobacterium tuberculosis is indispensable for arresting phagosomal maturation and growth of the pathogen in guinea pig tissues
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0070514
– volume: 599
  start-page: 290
  year: 2021
  end-page: 295
  ident: B50
  article-title: Shigella evades pyroptosis by arginine ADP-riboxanation of caspase-11
  publication-title: Nature
  doi: 10.1038/s41586-021-04020-1
– volume: 5
  start-page: 720
  year: 2003
  end-page: 726
  ident: B18
  article-title: Connexin-dependent inter-cellular communication increases invasion and dissemination of Shigella in epithelial cells
  publication-title: Nat Cell Biol
  doi: 10.1038/ncb1021
– volume: 9
  year: 2021
  ident: B25
  article-title: Modulation of OMV production by the lysis module of the DLP12 defective prophage of Escherichia coli K12
  publication-title: Microorganisms
  doi: 10.3390/microorganisms9020369
– volume: 12
  start-page: 1390
  year: 2005
  end-page: 1397
  ident: B15
  article-title: Cells die with increased cytosolic ATP during apoptosis: a bioluminescence study with intracellular luciferase
  publication-title: Cell Death Differ
  doi: 10.1038/sj.cdd.4401661
– volume: 6
  year: 2016
  ident: B53
  article-title: Implications of spatiotemporal regulation of Shigella flexneri type three secretion activity on effector functions: think globally, act locally
  publication-title: Front Cell Infect Microbiol
  doi: 10.3389/fcimb.2016.00028
– volume: 43
  start-page: 923
  year: 2015
  end-page: 932
  ident: B47
  article-title: Caspase-11 requires the pannexin-1 channel and the purinergic P2X7 pore to mediate pyroptosis and endotoxic shock
  publication-title: Immunity
  doi: 10.1016/j.immuni.2015.10.009
– volume: 90
  year: 2022
  ident: B14
  article-title: Reprogramming of cell death pathways by bacterial effectors as a widespread virulence strategy
  publication-title: Infect Immun
  doi: 10.1128/iai.00614-21
– volume: 148
  start-page: 2519
  year: 2002
  end-page: 2529
  ident: B7
  article-title: Enteroinvasive Escherichia coli virulence-plasmid-carried apyrase (apy) and ospB genes are organized as a bicistronic operon and are subject to differential expression
  publication-title: Microbiology (Reading)
  doi: 10.1099/00221287-148-8-2519
– volume: 10
  start-page: 863
  year: 2008
  end-page: 875
  ident: B37
  article-title: ATP scavenging by the intracellular pathogen porphyromonas gingivalis inhibits P2X7-mediated host-cell apoptosis
  publication-title: Cell Microbiol
  doi: 10.1111/j.1462-5822.2007.01089.x
– volume: 5
  year: 2020
  ident: B2
  article-title: Acinetobacter baumannii targets human carcinoembryonic antigen-related cell adhesion molecules (CEACAMs) for invasion of pneumocytes
  publication-title: mSystems
  doi: 10.1128/mSystems.00604-20
– volume: 21
  start-page: 305
  year: 2019
  end-page: 312
  ident: B3
  article-title: Colonic adenoma-associated Escherichia coli express specific phenotypes
  publication-title: Microbes Infect
  doi: 10.1016/j.micinf.2019.02.001
– volume: 19
  year: 2018
  ident: B21
  article-title: Unfolding role of a danger molecule adenosine signaling in modulation of microbial infection and host cell response
  publication-title: Int J Mol Sci
  doi: 10.3390/ijms19010199
– volume: 7
  year: 2012
  ident: B24
  article-title: Outer membrane protein A (OmpA): a new player in Shigella flexneri protrusion formation and inter-cellular spreading
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0049625
– volume: 59
  start-page: 1
  year: 2021
  end-page: 7
  ident: B22
  article-title: Shigella infection and host cell death: a double-edged sword for the host and pathogen survival
  publication-title: Curr Opin Microbiol
  doi: 10.1016/j.mib.2020.07.007
– volume: 514
  start-page: 187
  year: 2014
  end-page: 192
  ident: B46
  article-title: Inflammatory caspases are innate immune receptors for intracellular LPS
  publication-title: Nature
  doi: 10.1038/nature13683
– volume: 3
  year: 2016
  ident: B9
  article-title: The multifaceted activity of the VirF regulatory protein in the Shigella lifestyle
  publication-title: Front Mol Biosci
  doi: 10.3389/fmolb.2016.00061
– volume: 7
  year: 2019
  ident: B6
  article-title: Shigella pathogenesis: new insights through advanced methodologies
  publication-title: Microbiol Spectr
  doi: 10.1128/microbiolspec.BAI-0023-2019
– volume: 305
  start-page: 75
  year: 2015
  end-page: 84
  ident: B10
  article-title: The Shigella flexneri Ospb effector: an early Immunomodulator
  publication-title: Int J Med Microbiol
  doi: 10.1016/j.ijmm.2014.11.004
– volume: 178
  start-page: 1770
  year: 1996
  end-page: 1773
  ident: B27
  article-title: Sura assists the folding of Escherichia coli outer membrane proteins
  publication-title: J Bacteriol
  doi: 10.1128/jb.178.6.1770-1773.1996
– volume: 391
  start-page: 801
  year: 2018
  end-page: 812
  ident: B4
  article-title: Shigellosis
  publication-title: Lancet
  doi: 10.1016/S0140-6736(17)33296-8
– volume: 46
  start-page: 649
  year: 2017
  end-page: 659
  ident: B49
  article-title: NAIP-NLRC4 Inflammasomes coordinate intestinal epithelial cell expulsion with eicosanoid and IL-18 release via activation of caspase-1 and -8
  publication-title: Immunity
  doi: 10.1016/j.immuni.2017.03.016
– volume: 14
  start-page: 1271
  year: 2012
  end-page: 1277
  ident: B39
  article-title: Role of extracellular nucleotides in the immune response against intracellular bacteria and protozoan parasites
  publication-title: Microbes and Infection
  doi: 10.1016/j.micinf.2012.05.009
– volume: 79
  start-page: 414
  year: 2011
  end-page: 420
  ident: B36
  article-title: Coxiella burnetii acid phosphatase inhibits the release of reactive oxygen Intermediates in polymorphonuclear leukocytes
  publication-title: Infect Immun
  doi: 10.1128/IAI.01011-10
– volume: 265
  start-page: 130
  year: 2015
  end-page: 142
  ident: B29
  article-title: Pyroptotic cell death defends against intracellular pathogens
  publication-title: Immunol Rev
  doi: 10.1111/imr.12287
– volume: 21
  start-page: 707
  year: 2008
  end-page: 714
  ident: B8
  article-title: Evaluation by real-time PCR of the expression of S. flexneri virulence-associated genes ospB and phoN2 under different genetical backgrounds
  publication-title: Int J Immunopathol Pharmacol
  doi: 10.1177/039463200802100325
– volume: 8
  year: 2013
  ident: B35
  article-title: Type A Francisella tularensis acid phosphatases contribute to pathogenesis
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0056834
– volume: 15
  year: 2022
  ident: B17
  article-title: Pyroptosis in host defence against bacterial infection
  publication-title: Dis Model Mech
  doi: 10.1242/dmm.049414
– volume: 6
  year: 2021
  ident: B16
  article-title: Pyroptosis: mechanisms and diseases
  publication-title: Signal Transduct Target Ther
  doi: 10.1038/s41392-021-00507-5
– volume: 21
  start-page: 15
  year: 2020
  ident: B44
  article-title: Extracellular ATP as an inter-kingdom signaling molecule: release mechanisms by bacteria and its implication on the host
  publication-title: Int J Mol Sci
  doi: 10.3390/ijms21155590
– volume: 21
  start-page: 134
  year: 2008
  end-page: 156
  ident: B5
  article-title: Molecular pathogenesis of Shigella spp.: controlling host cell signaling, invasion, and death by type III secretion
  publication-title: Clin Microbiol Rev
  doi: 10.1128/CMR.00032-07
– volume: 205
  start-page: 125
  year: 2017
  end-page: 134
  ident: B40
  article-title: Nucleoside diphosphate kinase (Ndk): a pleiotropic effector manipulating bacterial virulence and adaptive responses
  publication-title: Microbiol Res
  doi: 10.1016/j.micres.2017.09.001
– volume: 8
  start-page: 168
  year: 2016
  end-page: 173
  ident: B12
  article-title: The Shigella flexneri OmpA amino acid residues 188EVQ190 are essential for the interaction with the virulence factor PhoN2
  publication-title: Biochem Biophys Rep
  doi: 10.1016/j.bbrep.2016.08.010
– volume: 243
  start-page: 206
  year: 2011
  end-page: 214
  ident: B28
  article-title: Caspase-1-induced pyroptotic cell death
  publication-title: Immunol Rev
  doi: 10.1111/j.1600-065X.2011.01044.x
– volume: 9
  year: 2020
  ident: B48
  article-title: NAIP-NLRC4-deficient mice are susceptible to shigellosis
  publication-title: Elife
  doi: 10.7554/eLife.59022
– volume: 289
  start-page: G407
  year: 2005
  end-page: 17
  ident: B19
  article-title: Two pathways for ATP release from host cells in enteropathogenic Escherichia coli infection
  publication-title: Am J Physiol Gastrointest Liver Physiol
  doi: 10.1152/ajpgi.00137.2005
– volume: 188
  start-page: 1620
  year: 2006
  end-page: 1627
  ident: B13
  article-title: Apyrase, the product of the virulence plasmid-encoded phoN2 (apy) gene of Shigella flexneri, is necessary for proper unipolar IcsA localization and for efficient Intercellular spread
  publication-title: J Bacteriol
  doi: 10.1128/JB.188.4.1620-1627.2006
– volume: 29
  start-page: 1521
  year: 2021
  end-page: 1530
  ident: B51
  article-title: Shigella ubiquitin ligase IpaH7.8 targets gasdermin D for degradation to prevent pyroptosis and enable infection
  publication-title: Cell Host Microbe
  doi: 10.1016/j.chom.2021.08.010
– volume: 10
  year: 2019
  ident: B52
  article-title: Evolutionary perspectives on the moonlighting functions of bacterial factors that support actin-based motility
  publication-title: mBio
  doi: 10.1128/mBio.01520-19
– volume: 22
  start-page: 3561
  year: 2020
  end-page: 3571
  ident: B33
  article-title: Developing robust protein analysis profiles to identify bacterial acid phosphatases in genomes and metagenomic libraries
  publication-title: Environ Microbiol
  doi: 10.1111/1462-2920.15138
– volume: 111
  start-page: 9929
  year: 2014
  end-page: 9934
  ident: B43
  article-title: Shigella reroutes host cell central metabolism to obtain high-flux nutrient supply for vigorous intracellular growth
  publication-title: Proc Natl Acad Sci U S A
  doi: 10.1073/pnas.1406694111
– volume: 6
  start-page: 38
  year: 2016
  ident: B1
  article-title: Cellular aspects of Shigella pathogenesis: focus on the manipulation of host cell processes
  publication-title: Front Cell Infect Microbiol
  doi: 10.3389/fcimb.2016.00038
– volume: 5
  year: 2014
  ident: B20
  article-title: Extracellular ATP drives systemic inflammation, tissue damage and mortality
  publication-title: Cell Death Dis
  doi: 10.1038/cddis.2014.70
– volume: 307
  start-page: 268
  year: 2017
  end-page: 275
  ident: B23
  article-title: Role of the SRRz/Rz1 lambdoid lysis cassette in the pathoadaptive evolution of Shigella
  publication-title: Int J Med Microbiol
  doi: 10.1016/j.ijmm.2017.03.002
– volume: 80
  start-page: 1088
  year: 2012
  end-page: 1097
  ident: B38
  article-title: The acid phosphatase AcpA is secreted in vitro and in macrophages by Francisella spp
  publication-title: Infect Immun
  doi: 10.1128/IAI.06245-11
– volume: 53
  start-page: 1768
  year: 2012
  end-page: 1775
  ident: B45
  article-title: Changes in cytosolic ATP levels and intracellular morphology during bacteria-induced Hypersensitive cell death as revealed by real-time fluorescence microscopy imaging
  publication-title: Plant Cell Physiol
  doi: 10.1093/pcp/pcs119
– volume: 54
  start-page: 833
  year: 1998
  end-page: 850
  ident: B31
  article-title: Bacterial nonspecific acid phosphohydrolases: physiology, evolution and use as tools in microbial biotechnology
  publication-title: Cell Mol Life Sci
  doi: 10.1007/s000180050212
– volume: 9
  start-page: 508
  year: 2011
  end-page: 519
  ident: B41
  article-title: ATP-mediated Erk1/2 activation stimulates bacterial capture by filopodia, which precedes Shigella invasion of epithelial cells
  publication-title: Cell Host Microbe
  doi: 10.1016/j.chom.2011.05.005
– volume: 39
  start-page: 1121
  year: 2013
  end-page: 1131
  ident: B42
  article-title: A Shigella effector dampens inflammation by regulating epithelial release of danger signal ATP through production of the lipid mediator PtdIns5P
  publication-title: Immunity
  doi: 10.1016/j.immuni.2013.11.013
– volume: 79
  year: 2021
  ident: B30
  article-title: Keeping the host alive - lessons from obligate intracellular bacterial pathogens
  publication-title: Pathog Dis
  doi: 10.1093/femspd/ftab052
– volume: 16
  start-page: 291
  year: 1995
  end-page: 300
  ident: B26
  article-title: Enhanced secretion through the Shigella flexneri Mxi-Spa translocon leads to assembly of extracellular proteins into macromolecular structures
  publication-title: Mol Microbiol
  doi: 10.1111/j.1365-2958.1995.tb02301.x
– volume: 9
  year: 2014
  ident: B11
  article-title: Polar localization of PhoN2, a periplasmic virulence-associated factor of Shigella flexneri, is required for proper IcsA exposition at the old bacterial pole
  publication-title: PLoS One
  doi: 10.1371/journal.pone.0090230
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Snippet Intestinal epithelial cells represent the first line of defense from invading enteric pathogens. During the course of infection, pro-inflammatory programmed...
In this paper, we demonstrated that apyrase is released within the host cell cytoplasm during infection to target the intracellular ATP pool. By degrading...
ABSTRACT Intestinal epithelial cells represent the first line of defense from invading enteric pathogens. During the course of infection, pro-inflammatory...
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StartPage e0077523
SubjectTerms apyrase
ATP
Clinical Microbiology
host cell survival
inflammation
pyroptosis
Research Article
Shigella flexneri
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Title The Shigella flexneri virulence factor apyrase is released inside eukaryotic cells to hijack host cell fate
URI https://www.ncbi.nlm.nih.gov/pubmed/37795996
https://journals.asm.org/doi/10.1128/spectrum.00775-23
https://www.proquest.com/docview/2873252286
https://pubmed.ncbi.nlm.nih.gov/PMC10714728
https://doaj.org/article/7ccb2819d8c0495d9af1bb1fce3b45dc
Volume 11
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