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1. List of contributors

Author

Aizawa, Shin-Ichi, primary, Alberdi, Pilar, additional, Alexander, David C., additional, Alía, Alberto, additional, Allison, D.G., additional, Amyes, Sebastian G.B., additional, An, Haoran, additional, Andrade, María J., additional, Antelmann, Haike, additional, Arias, Cesar A., additional, Asensio, Miguel A., additional, Axell-House, Dierdre B., additional, Bae, Hee-Won, additional, Baena, Laura Muñoz, additional, Baig, Abdul Mannan, additional, Bailey, Spenser O., additional, Baize, Sylvain, additional, Baldi, Pablo C., additional, Barbosa, Angela Silva, additional, Barbuddhe, Sukhadeo B., additional, Bard, Emilie, additional, Barry, Eileen M., additional, Basarab, Gregory S., additional, Beloborodova, N.V, additional, Bermúdez, Elena, additional, Bidmos, Fadil A., additional, Bisgaard, Magne, additional, Blakely, Garry W., additional, Bloch, Evan, additional, Boesen, Thias Oberg, additional, Bose, Dipayan, additional, Botero, Javier Enrique, additional, Bouabe, Hicham, additional, Bouchard, Michael J., additional, Bozue, Joel A., additional, Bradbury, Richard S., additional, Brett Moreau, G., additional, Cabezas-Cruz, Alejandro, additional, Cai, Rong-Jun, additional, Calderón, Enrique J., additional, Cao, Boyang, additional, Carmena, David, additional, Carvalho, Eneas, additional, Caulfield, Amanda D., additional, Cen, Shan, additional, Chai, Jong-Yil, additional, Chamberland, Robin R., additional, Champredon, David, additional, Chan, Edward D., additional, Charbon, Godefroid, additional, Chato, Connor, additional, Chelomina, G.N., additional, Chen, Jingyu, additional, Chen, Min, additional, Chen, Shuyu, additional, Chen, Suilin, additional, Chen, Yanfei, additional, Chen, Zhaoyuan, additional, Cheng, Aimin, additional, Cheng, Keding, additional, Chiu, Charles Y., additional, Cho, You-Hee, additional, Christensen, Henrik, additional, Chrtdernevskaya, E.A., additional, Contreras, Adolfo, additional, Contreras, Marinela, additional, Córdoba, Juan J., additional, Córdoba, María G., additional, Costa, Rita, additional, Cote, Christopher K., additional, Cui, Xiangling, additional, Cui, Yujun, additional, Dacal, Elena, additional, Dammann, Allison N., additional, Das, Shubhagata, additional, Dashti, Alejandro, additional, de la Fuente, José, additional, de la Garza, Mireya, additional, Delgado, Josué, additional, Delgado-Cuesta, Juan, additional, Deng, Haiteng, additional, Deng, Li, additional, Dey, Debajit, additional, Dhama, Kuldeep, additional, Diego, Juan García-Bernalt, additional, Ding, Hao, additional, Doern, Christopher D., additional, Dorman, Charles J., additional, Du, Zongmin, additional, Dunbar, Sherry A., additional, Duthie, Malcolm, additional, Dybvig, Kevin F., additional, Eakin, Ann E., additional, Eallonardo, Samuel J., additional, Eberly, Allison R., additional, Echeverry, Adriana Jaramillo, additional, Egland, Paul G., additional, El Zowalaty, Mohamed E., additional, Endsley, Janice Jones, additional, Eom, Keeseon S., additional, Evans, Benjamin A., additional, Falkinham, Joseph O., additional, Feng, Siwei, additional, Feng, Yaoyu, additional, Feng, Zongdi, additional, Fernández-Soto, Pedro, additional, Ferreira, Roux-Cil, additional, Flores-Huerta, Nadia, additional, Foster, Timothy J., additional, Fox-Moon, Sandra M., additional, Fraga, Tatiana Rodrigues, additional, Fredricks, David N., additional, Freitag, Nancy E., additional, Frimodt-Møller, Jakob, additional, Fuller, Risa, additional, Ganesh, Balasubramanian, additional, Gao, Ning, additional, García-Carnero, Laura C., additional, Garzetti, Debora, additional, Geoghegan, Joan A., additional, Ghenim, Raed, additional, Giambartolomei, Guillermo H., additional, Gilbert, Nicole M., additional, Gillis, Thomas Phillip, additional, Gladstone, Camilla A., additional, Gómez-Gaviria, Manuela, additional, Gómez-Marín, Jorge E., additional, Gong, Tengfang, additional, González, Ramón A., additional, Gray-Owen, Scott D., additional, Gu, Bing, additional, Guzmán-Téllez, Paula, additional, Hajal, Caroline, additional, Han, Yanping, additional, Hao, Yi, additional, Harrington, Amanda T., additional, Harris, Jason B., additional, Harvill, Eric T., additional, Hasan, S. Saif, additional, He, Guang-Jun, additional, He, Yongqun, additional, Heffron, Jared D., additional, Hidalgo, Paloma, additional, Hindiyeh, Musa Y., additional, Hreha, Teri N., additional, Hu, Xiaoyu, additional, Huang, Guanghua, additional, Huang, Jiangqing, additional, Huang, Liang, additional, Huang, Shifeng, additional, Huang, Xingxu, additional, Huang, Xueting, additional, Huang, Yilun, additional, Huffman, Anthony, additional, Humphreys, Tricia L., additional, Hunstad, David A., additional, Inglis, Timothy J.J., additional, Isaac, Lourdes, additional, Jacobs, Samantha E., additional, Janowicz, Diane M., additional, Jeon, Hyeong-Kyu, additional, Ji, Quanjiang, additional, Jia, Qi, additional, Jia, Wei, additional, Jin, Shouguang, additional, Jneidi, Lama, additional, Jose, Shinsmon, additional, Jung, Bong-Kwang, additional, Kattan, Randa, additional, Kaushik, Rahul, additional, Khare, Reeti, additional, Kim, Eun Sook, additional, Kirn, Thomas J., additional, Koo, Hyun, additional, Köster, Pamela C., additional, Krause, Peter J., additional, Kumar, Sanjai, additional, Kupz, Andreas, additional, Lambert, P.A., additional, Lamont, Richard J., additional, Langford, Paul R., additional, Lebeaux, David, additional, Legname, Giuseppe, additional, Li, Bin, additional, Li, Chunhao, additional, Li, Fen, additional, Li, Jun, additional, Li, Lanjuan, additional, Li, Ruofan, additional, Li, Ruoyu, additional, Li, Ting, additional, Li, Yang-Yang, additional, Li, Yanhua, additional, Li, Zhuorong, additional, Liang, Xiaomeng, additional, Liao, Guojian, additional, Lin, Ping, additional, Ling, Yun, additional, Liu, Bo, additional, Liu, Dongyou, additional, Liu, Guohua, additional, Liu, Huidi, additional, Liu, Jiafeng, additional, Liu, Jintao, additional, Liu, Qi, additional, Liu, Shu-Lin, additional, Liu, Taiping, additional, Liu, Tongbao, additional, Liu, Wei, additional, Liu, Yan, additional, Liu, Yanni, additional, Liu, Yisong, additional, Liu, Yuan, additional, Løbner-Olesen, Anders, additional, Loeffelholz, Michael, additional, Lu, Hongzhou, additional, Luna, Brian, additional, Ma, Bingting, additional, Ma, Chengying, additional, Ma, Shuang, additional, Ma, TianLi, additional, Madan, Rajat, additional, Mahle, Rachael E., additional, Mahlen, Steven D., additional, Malik, Satya Veer Singh, additional, Malik, Yashpal Singh, additional, Malvy, Denis, additional, Mann, Barbara J., additional, Marasini, Daya, additional, Maris, Alexander S., additional, Marjomäki, Varpu, additional, Marjuki, Henju, additional, Martín, Alberto, additional, Martín, Irene, additional, Martínez-Castillo, Moisés, additional, Martínez-Pabón, María Cecilia, additional, Mathison, Blaine A., additional, Ma’ayeh, Showgy, additional, McDowell, Andrew, additional, McLaughlin, Stephanie E., additional, McSheffrey, Gordon G., additional, Medrano, Francisco J., additional, Meehan, Conor J., additional, Mehta, Dhwani, additional, Mejía-Oquendo, Manuela, additional, Melo-Cristino, José, additional, Mendoza-Barberá, Elena, additional, Meng, Xinan, additional, Merino, Susana, additional, Merritt, Adam J., additional, Miller, Steve, additional, Miller, William R., additional, Minamino, Tohru, additional, Mirzaei, Mohammadali Khan, additional, Mora-Montes, Héctor M., additional, Mortensen, Joel, additional, Mostafa, Heba H., additional, Muhsen, Khitam, additional, Mujahed, Ahlam, additional, Muro, Antonio, additional, Murphy, Olwen C., additional, Newton, Hayley J., additional, Nguyen, April H., additional, Nichols, Wright W., additional, Niu, Siqiang, additional, Núñez, Félix, additional, Obregon, Dasiel, additional, Okamoto, Akira, additional, Okutani, Akiko, additional, Olabode, Abayomi, additional, Omar, Muna, additional, Ong, Edison, additional, Ouyang, Zhiming, additional, Pacak, Christina A., additional, Pacheco-Yépez, Judith, additional, Palmer, John, additional, Pang, Xiaoli, additional, Paredes-Sabja, Daniel, additional, Peng, Zhong, additional, Peng, Zonggen, additional, Pérez-Nevado, Francisco, additional, Poon, Art, additional, Pospíšilová, Petra, additional, Potts, Caelin C., additional, Pu, Qinqin, additional, Pujic, Petar, additional, Qi, Rui, additional, Qian, Chenyun, additional, Qian, Liu, additional, Qin, Aiping, additional, Qu, Fen, additional, Rakin, Alexander, additional, Ramesh, Ashwin, additional, Ramirez, Mario, additional, Rao, Yu, additional, Ratner, Adam J., additional, Rawool, Deepak B., additional, Rehman, Asma, additional, Ren, Jie, additional, Ren, Ping, additional, Retchless, Adam C., additional, Robertson, Erle S., additional, Rodríguez, Alicia, additional, Rodriguez, Azucena, additional, Rodríguez-Medina, Carolina, additional, Rodriguez-Nava, Veronica, additional, Rohde, Manfred, additional, Romero-Rodríguez, Alba, additional, Rosales-Morgan, Gabriela, additional, Rosenkranz, Andrea L., additional, Ruiz-Moyano, Santiago, additional, Ruokolainen, Visa, additional, Sabateen, Ali, additional, Sahu, Radhakrishna, additional, Sails, Andrew, additional, Sang, Yu, additional, Santana, Clarissa H., additional, Santos, Jesus A., additional, Santos, Renato L., additional, Schmitz, Jonathan E., additional, Serrano-Luna, Jesús, additional, Shen, Jianzhong, additional, Shen, Zhangqi, additional, Shibayama, Mineko, additional, Shirtliff, Mark E., additional, Silva-Costa, Catarina, additional, Silva-Olivares, Angélica, additional, Singh, Niraj Kumar, additional, Šmajs, David, additional, Smith, Robert P., additional, Smith, Sophie, additional, Snyder, Lori A.S., additional, Song, Yinggai, additional, Soro, Aurea Simon, additional, Spearman, Paul, additional, Spellberg, Brad, additional, Sprague, Lisa D., additional, Stratton, Charles W., additional, Strenk, Susan M., additional, Strugnell, Richard A., additional, Sun, Keer, additional, Suo, Xun, additional, Suzuki-Hatano, Silveli, additional, Svärd, Staffan, additional, Talbot, Elizabeth A., additional, Tamez-Castrellón, Alma K., additional, Tan, Nie, additional, Tang, Cynthia Y., additional, Tang, Yi-Wei, additional, Tao, Jia, additional, Tao, Lili, additional, Terrero-Salcedo, David, additional, Tharmalingam, Jayaraman, additional, Thwe, Phyu M., additional, Tiamani, Kawtar, additional, Tomás, Juan M., additional, Topaz, Nadav, additional, Tsai, Ang-Chen, additional, Tsalik, Ephraim L., additional, Tuomanen, Elaine I., additional, Turenne, Christine Y., additional, Tyagi, Anuj, additional, Uprety, Priyanka, additional, Valour, Florent, additional, van Hensbergen, Vincent P., additional, Venkatesan, Arun, additional, Vergis, Jess, additional, Villar, Margarita, additional, Vollmer, Waldemar, additional, Waites, Ken B., additional, Wan, Xiu-Feng, additional, Wang, Guiqing, additional, Wang, Lijun, additional, Wang, Lin, additional, Wang, Linqi, additional, Wang, Xiangru, additional, Wang, Xin, additional, Wang, Xinjie, additional, Wang, Ya-Ting, additional, Wang, Yang, additional, Wang, Yating, additional, Weil, Ana A., additional, Welkos, Susan L., additional, Wengenack, Nancy L., additional, Westblade, Lars F., additional, Whitfield, Chris, additional, Wu, Hui, additional, Wu, Lijuan, additional, Wu, Min, additional, Wu, Yarong, additional, Wu, Zhaowei, additional, Xiang, Ye, additional, Xiao, Di, additional, Xiao, Li, additional, Xiao, Lihua, additional, Xu, Tao, additional, Xu, Wenyue, additional, Xu, Xinping, additional, Xue, Jinling, additional, Yadav, Jay Prakash, additional, Yan, Junxiang, additional, Yan, Yixin, additional, Yang, Changmei, additional, Yang, Ruifu, additional, Yang, Ying, additional, Yao, Kaihu, additional, Yao, Yu-Feng, additional, Yeakle, Kyle C., additional, Yu, Demin, additional, Yu, Hao, additional, Yu, Xue-Jie, additional, Yuan, Zhenghong, additional, Zai, Wenjing, additional, Zhang, Jianzhong, additional, Zhang, Jing-Ren, additional, Zhang, Lanyue, additional, Zhang, Lijie, additional, Zhang, Qiwei, additional, Zhang, Wenbao, additional, Zhang, Wenhong, additional, Zhang, Xinxin, additional, Zhao, Youbao, additional, Zhou, Chuanmin, additional, Zhu, Feng, additional, Zhu, Jingting, additional, and Zhu, Yongqun, additional

Published
2024
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6. Contributors

Author

Alvarez, Beatriz, primary, Antelmann, Haike, additional, Arnér, Elias S.J., additional, Aschner, Michael, additional, Bandyopadhyay, Tirthankar, additional, Banerjee, Ruma, additional, Benchoam, Dayana, additional, Berkmen, Mehmet, additional, Berndt, Carsten, additional, Bodnar, Yana, additional, de Bont, Linda, additional, Bortoli, Marco, additional, Carballal, Sebastián, additional, Carroll, Kate S., additional, Comini, Marcelo A., additional, Cuevasanta, Ernesto, additional, Denicola, Ana, additional, Deponte, Marcel, additional, Dick, Tobias P., additional, Eaglesham, James B., additional, Ezeriņa, Daria, additional, Ferrer-Sueta, Gerardo, additional, Forshaw, Tom E., additional, Fritsch, Verena Nadin, additional, Furdui, Cristina M., additional, Garcia, Augusto, additional, Gellert, Manuela, additional, Gladyshev, Vadim N., additional, Jacquot, Jean-Pierre, additional, Leichert, Lars I., additional, Lillig, Christopher Horst, additional, Lundstedt, Emily, additional, Manta, Bruno, additional, Marino, Stefano M., additional, Mariotti, Marco, additional, Messens, Joris, additional, Möller, Matías N., additional, Morgan, Bruce, additional, Netto, Luis E.S., additional, Nogara, Pablo A., additional, Oliveira, Cláudia S., additional, de Oliveira, Marcos Antonio, additional, Orian, Laura, additional, Orrico, Florencia, additional, Outten, Caryn E., additional, Pereira, Meire E., additional, Racho, Julia, additional, Radi, Rafael, additional, Randall, Lía M., additional, Riemer, Jan, additional, Rocha, João B.T., additional, Rouhier, Nicolas, additional, Salinas, Gustavo, additional, Schöneich, Christian, additional, Schopfer, Francisco J., additional, Shi, Yunlong, additional, Steglich, Martina, additional, Tairum, Carlos A., additional, Talwar, Deepti, additional, Thomson, Leonor, additional, Trujillo, Madia, additional, Tsang, Allen W., additional, Turell, Lucía, additional, Villar, Sebastián, additional, Vitturi, Dario A., additional, Weiss, Konstantin, additional, Wilms, Christina, additional, Zeida, Ari, additional, and Zimmermann, Jannik, additional

Published
2022
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8. The MarR/DUF24-Family QsrR Repressor Senses Quinones and Oxidants by Thiol Switch Mechanisms in Staphylococcus aureus

Author

Fritsch, Verena Nadin, Van Loi, Vu, Kuropka, Benno, Gruhlke, Martin C. H., Weise, Christoph, and Antelmann, Haike

Subjects
thiol-switch, Staphylococcus aureus, quinones, Physiology, Clinical Biochemistry, ROS, HOCl, 500 Naturwissenschaften und Mathematik::570 Biowissenschaften, Biologie::570 Biowissenschaften, Biologie, Cell Biology, Biochemistry, QsrR, RES, ddc:540, General Earth and Planetary Sciences, Molecular Biology, General Environmental Science
Abstract

Antioxidants & redox signaling : ARS 10, ars.2022.0090 (2022). doi:10.1089/ars.2022.0090, Published by Liebert, Larchmont, NY

Published
2023

22. The MerR‐family regulator NmlR is involved in the defense against oxidative stress in Streptococcus pneumoniae.

Author

Fritsch, Verena Nadin, Linzner, Nico, Busche, Tobias, Said, Nelly, Weise, Christoph, Kalinowski, Jörn, Wahl, Markus C., and Antelmann, Haike

Subjects
STREPTOCOCCUS pneumoniae, GENE expression profiling, OXIDATIVE stress, MASS spectrometry, HYPOCHLORITES
Abstract

Streptococcus pneumoniae has to cope with the strong oxidant hypochlorous acid (HOCl), during host–pathogen interactions. Thus, we analyzed the global gene expression profile of S. pneumoniae D39 towards HOCl stress. In the RNA‐seq transcriptome, the NmlR, SifR, CtsR, HrcA, SczA and CopY regulons and the etrx1‐ccdA1‐msrAB2 operon were most strongly induced under HOCl stress, which participate in the oxidative, electrophile and metal stress response in S. pneumoniae. The MerR‐family regulator NmlR harbors a conserved Cys52 and controls the alcohol dehydrogenase‐encoding adhC gene under carbonyl and NO stress. We demonstrated that NmlR senses also HOCl stress to activate transcription of the nmlR‐adhC operon. HOCl‐induced transcription of adhC required Cys52 of NmlR in vivo. Using mass spectrometry, NmlR was shown to be oxidized to intersubunit disulfides or S‐glutathionylated under oxidative stress in vitro. A broccoli‐FLAP‐based assay further showed that both NmlR disulfides significantly increased transcription initiation at the nmlR promoter by RNAP in vitro, which depends on Cys52. Phenotype analyses revealed that NmlR functions in the defense against oxidative stress and promotes survival of S. pneumoniae during macrophage infections. In conclusion, NmlR was characterized as HOCl‐sensing transcriptional regulator, which activates transcription of adhC under oxidative stress by thiol switches in S. pneumoniae. [ABSTRACT FROM AUTHOR]

Published
2023
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23. The Catalase KatA Contributes to Microaerophilic H2O2 Priming to Acquire an Improved Oxidative Stress Resistance in Staphylococcus aureus

Author

Linzner, Nico, Loi, Vu Van, and Antelmann, Haike

Subjects
Staphylococcus aureus, AhpC, Bcp, H2O2 resistance, Tpx, KatA, 500 Naturwissenschaften und Mathematik::570 Biowissenschaften, Biologie::570 Biowissenschaften, Biologie, priming
Abstract

Staphylococcus aureus has to cope with oxidative stress during infections. In this study, S. aureus was found to be resistant to 100 mM H2O2 during aerobic growth. While KatA was essential for this high aerobic H2O2 resistance, the peroxiredoxin AhpC contributed to detoxification of 0.4 mM H2O2 in the absence of KatA. In addition, the peroxiredoxins AhpC, Tpx and Bcp were found to be required for detoxification of cumene hydroperoxide (CHP). The high H2O2 tolerance of aerobic S. aureus cells was associated with priming by endogenous H2O2 levels, which was supported by an oxidative shift of the bacillithiol redox potential to −291 mV compared to −310 mV in microaerophilic cells. In contrast, S. aureus could be primed by sub-lethal doses of 100 µM H2O2 during microaerophilic growth to acquire an improved resistance towards the otherwise lethal triggering stimulus of 10 mM H2O2. This microaerophilic priming was dependent on increased KatA activity, whereas aerobic cells showed constitutive high KatA activity. Thus, KatA contributes to the high H2O2 resistance of aerobic cells and to microaerophilic H2O2 priming in order to survive the subsequent lethal triggering doses of H2O2, allowing the adaptation of S. aureus under infections to different oxygen environments.

Published
2022

27. The Effect of Allicin on the Proteome of SARS-CoV-2 Infected Calu-3 Cells

Author

Mösbauer, Kirstin, Fritsch, Verena Nadin, Adrian, Lorenz, Bernhardt, Jörg, Gruhlke, Martin C. H., Slusarenko, Alan, Niemeyer, Daniela, and Antelmann, Haike

Subjects
Vero E6, Calu-3, SARS-CoV-2, ddc:570, proteome, allicin, Microbiology, Original Research
Abstract

Frontiers in microbiology 12, 746795 (2021). doi:10.3389/fmicb.2021.746795, Published by Frontiers Media, Lausanne

Published
2021

29. List of Contributors

Author

Abel-Santos, Ernesto, primary, Abraham, Soman N., additional, Aizawa, Shin-Ichi, additional, Aldape, Michael J., additional, Alexander, David C., additional, Allison, David G., additional, Amyes, Sebastian G.B., additional, Anderson, Burt E., additional, Anderson, Frank J., additional, Antelmann, Haike, additional, Austin, Frank W., additional, Ayllón, Nieves, additional, Bai, Fang, additional, Barbosa, Angela Silva, additional, Barer, Michael R., additional, Basarab, Gregory S., additional, Beaman, Blaine L., additional, Beard, Matthew, additional, Black, Carolyn M., additional, Blakely, Garry W., additional, Boiron, Patrick, additional, Bouabe, Hicham, additional, Bozue, Joel A., additional, Brinkman, Cassandra L., additional, Brubaker, Robert R., additional, Bryant, Amy E., additional, Cain, Robert J., additional, Calvo, Ana Cristina, additional, Carvalho, Eneas, additional, Capo, Christian, additional, Castillo-Ramirez, Santiago, additional, Chaddock, John A., additional, Chamberland, Robin R., additional, Clarridge, Jill E., additional, Cote, Christopher K., additional, Cox, Sarah L., additional, Cutler, Sally J., additional, Davidson, Donald J., additional, Day, Nicholas P.J., additional, de la Fuente, José, additional, De Jesus, Magdia, additional, Dorin, Julia R., additional, Dorman, Charles J., additional, Eakin, Ann E., additional, Egland, Paul G., additional, Ellis, Simon, additional, Enright, Mark C., additional, Evans, Benjamin A., additional, Everett, Jake A., additional, Falkinham, Joseph O., additional, Fan, Feinan, additional, Fan, Huizhou, additional, Faulds-Pain, Alexandra, additional, Feil, Edward J., additional, Figueroa, Cesar J., additional, Forsberg, Åke, additional, Foster, Timothy J., additional, Fox-Moon, Sandra M., additional, Fraga, Tatiana Rodrigues, additional, Fredricks, David N., additional, Freitag, Nancy E., additional, García-López, María-Luisa, additional, Garzetti, Debora, additional, Gemmell, Curtis G., additional, Geoghegan, Joan A., additional, Gillis, Thomas P., additional, Gilmore, Michael S., additional, Goldstone, Robert J., additional, Gray-Owen, Scott D., additional, Guiso, Nicole, additional, Hallstrom, Kelly N., additional, Harper, David R., additional, Harrington, Amanda T., additional, Harris, Jason B., additional, Hays, John P., additional, He, Yongqun, additional, Heffron, Jared D., additional, Heimer, Susan R., additional, High, Nicola J., additional, Hobot, Jan A., additional, Hultgren, Scott, additional, Humphreys, Tricia L., additional, Hunstad, David A., additional, Igietseme, Joseph U., additional, Inglis, Neil F., additional, Inglis, Tim J.J., additional, Isaac, Lourdes, additional, Janowicz, Diane M., additional, Jin, Shouguang, additional, Jin, Yongxin, additional, Johansson, Anna-Lena, additional, Johnston, Randal N., additional, Jones, Jessica L., additional, Justice, Sheryl S., additional, Kaakoush, Nadeem O., additional, Kalas, Vasilios, additional, Khare, Reeti, additional, Jordan, I. King, additional, Kobayashi, Keiko, additional, Kocan, Katherine M., additional, Könönen, Eija, additional, Kumar, Purnima S., additional, Lambert, Peter A., additional, Lamont, Richard J., additional, Lan, Ruiting, additional, Lang, Sue, additional, Lereclus, Didier, additional, Levett, Paul N., additional, Li, Xuefeng, additional, Liu, Dongyou, additional, Liu, Shu-Lin, additional, Ma, Lin, additional, Mahlen, Steven D., additional, Man, Si Ming, additional, Margolis, Elisa, additional, Marrie, Thomas J., additional, Martin, Melissa J., additional, Mayer, Leonard W., additional, McConville, Malcolm, additional, McCormick, Beth A., additional, McDowell, Andrew, additional, McHugh, Brian J., additional, McMullen, P. David, additional, McSheffrey, Gordon G., additional, Mege, Jean-Louis, additional, Merritt, Adam J., additional, Minnick, Michael F., additional, Mitchell, Hazel M., additional, Morrison, Donald, additional, Musser, Kimberlee A., additional, Nagahama, Masahiro, additional, Nagao, Prescilla Emy, additional, Nagy, István, additional, Salomonsson, Emelie Näslund, additional, Nazarian, Elizabeth J., additional, Nichols, Wright W., additional, Noppa, Laila, additional, Octavia, Sophie, additional, Oda, Masataka, additional, Ofek, Itzhak, additional, Oliver, James D., additional, Olson, Patrick D., additional, Omosun, Yusuf, additional, Ong, Edmund, additional, Osta, Rosario, additional, Otero, Andrés, additional, Oyston, Petra C.F., additional, Paris, Daniel H., additional, Patel, Robin, additional, Patrick, Sheila, additional, Pedra, Joao H.F., additional, Posteraro, Brunella, additional, Posteraro, Patrizia, additional, Poxton, Ian R., additional, Pujic, Petar, additional, Raffa, Brittany J., additional, Rakin, Alexander, additional, Ramarao, Nalini, additional, Ramirez, Mario, additional, Ravalison, Miora, additional, Reed, Kurt D., additional, Reglinski, Mark, additional, Richards, Allen L., additional, Riesbeck, Kristian, additional, Riley, Thomas V., additional, Rodríguez-Calleja, José-María, additional, Rodríguez-Nava, Verónica, additional, Rumbaugh, Kendra P., additional, Sanderson, Kenneth E., additional, Sanguinetti, Maurizio, additional, Santos, Jesús A., additional, Santos, Renato L., additional, Schaar, Viveka, additional, Scheld, W. Michael, additional, Schmitz, Jonathan E., additional, Schwartzman, Joseph D., additional, Severo, Maiara S., additional, Sharon, Nathan, additional, Shirtliff, Mark E., additional, Simner, Patricia J., additional, Šmajs, David, additional, Smith, David G.E., additional, Sorokin, Alexei, additional, Sprague, Lisa D., additional, Sriskandan, Shiranee, additional, Stevens, Dennis L., additional, Stratton, Charles W., additional, Strouhal, Michal, additional, Su, Yu Ching, additional, Sussman, Max, additional, Talbot, Elizabeth A., additional, Tang, Le, additional, Tang, Yi-Wei, additional, Taur, Ying, additional, Tessier, Jeffrey M., additional, Textoris, Julien, additional, Thirumalapura, Nagaraja R., additional, Tsuge, Hideaki, additional, Turenne, Christine Y., additional, Valvano, Miguel A., additional, Vázquez-Boland, José A., additional, Verhaegh, Suzanne J.C., additional, Volkan, Ender, additional, Vollmer, Waldemar, additional, Wade, William F., additional, Waites, Ken B., additional, Walker, Alan W., additional, Walker, David H., additional, Wang, Guiqing, additional, Wang, Qinning, additional, Wang, Xin, additional, Ward, Bruce, additional, Watson, Eleanor, additional, Weil, Ana A., additional, Welkos, Susan L., additional, Wen, Zhensong, additional, Wengenack, Nancy L., additional, Westblade, Lars F., additional, Wexler, Hannah M., additional, Wren, Brendan W., additional, Wu, Min, additional, Wu, Shangwei, additional, Wu, Weihui, additional, Xiao, Li, additional, Zhang, Jing-Ren, additional, Zhao, Zuotao, additional, and Zhong, Guangming, additional

Published
2015
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32. The Catalase KatA Contributes to Microaerophilic H 2 O 2 Priming to Acquire an Improved Oxidative Stress Resistance in Staphylococcus aureus.

Author

Linzner, Nico, Loi, Vu Van, and Antelmann, Haike

Subjects
OXIDATIVE stress, CATALASE, REDUCTION potential, PEROXIREDOXINS, METABOLIC detoxification
Abstract

Staphylococcus aureus has to cope with oxidative stress during infections. In this study, S. aureus was found to be resistant to 100 mM H2O2 during aerobic growth. While KatA was essential for this high aerobic H2O2 resistance, the peroxiredoxin AhpC contributed to detoxification of 0.4 mM H2O2 in the absence of KatA. In addition, the peroxiredoxins AhpC, Tpx and Bcp were found to be required for detoxification of cumene hydroperoxide (CHP). The high H2O2 tolerance of aerobic S. aureus cells was associated with priming by endogenous H2O2 levels, which was supported by an oxidative shift of the bacillithiol redox potential to −291 mV compared to −310 mV in microaerophilic cells. In contrast, S. aureus could be primed by sub-lethal doses of 100 µM H2O2 during microaerophilic growth to acquire an improved resistance towards the otherwise lethal triggering stimulus of 10 mM H2O2. This microaerophilic priming was dependent on increased KatA activity, whereas aerobic cells showed constitutive high KatA activity. Thus, KatA contributes to the high H2O2 resistance of aerobic cells and to microaerophilic H2O2 priming in order to survive the subsequent lethal triggering doses of H2O2, allowing the adaptation of S. aureus under infections to different oxygen environments. [ABSTRACT FROM AUTHOR]

Published
2022
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35. The paralogous MarR/DUF24-family repressors YodB and CatR control expression of the catechol dioxygenase CatE in Bacillus subtilis

Author

Chi, Bui Khanh, Kobayashi, Kazuo, Albrecht, Dirk, Hecker, Michael, and Antelmann, Haike

Subjects
Quinone -- Properties, Catechin -- Properties, Genetic regulation -- Research, Gene expression -- Physiological aspects, Proteins -- Crosslinking, Proteins -- Research, Biological sciences
Abstract

The redox-sensing MarR/DUF24-type repressor YodB controls expression of the azoreductase AzoR1 and the nitroreductase YodC that are involved in detoxification of quinones and diamide in Bacillus subtilis. In the present paper, we identified YodB and its paralog YvaP (CatR) as repressors of the yfiDE (catDE) operon encoding a catechol-2,3-dioxygenase that also contributes to quinone resistance. Inactivation of both CatR and YodB is required for full derepression of catDE transcription. DNA-binding assays and promoter mutagenesis studies showed that CatR protects two inverted repeats with the consensus sequence TTAC-[N.sub.5]-GTAA overlapping the -35 promoter region (BS1) and the transcriptional start site (TSS) (BS2). The BS1 operator was required for binding of YodB in vitro. CatR and YodB share the conserved N-terminal Cys residue, which is required for redox sensing of CatR in vivo as shown by Cys-to-Ser mutagenesis. Our data suggest that CatR is modified by intermolecular disulfide formation in response to diamide and quinones in vitro and in vivo. Redox regulation of CatR occurs independently of YodB, and no protein interaction was detected between CatR and YodB in vivo using protein cross-linking and mass spectrometry. doi: 10.1128/JB.00409-10

Published
2010

36. Synthetic effects of secG and secY2 mutations on exoproteome biogenesis in Staphylococcus aureus

Author

Sibbald, Mark J.J.B., Winter, Theresa, van der Kooi-Pol, Magdalena M., Buist, G., Tsompanidou, E., Bosma, Tjibbe, Schafer, Tina, Ohlsen, Knut, Hecker, Michael, Antelmann, Haike, Engelmann, Susanne, and van Dijl, Jan Maarten

Subjects
Staphylococcus aureus -- Physiological aspects, Staphylococcus aureus -- Genetic aspects, Bacterial proteins -- Properties, Bacterial proteins -- Genetic aspects, Microbiological synthesis -- Research, Biological sciences
Abstract

The Gram-positive pathogen Staphylococcus aureus secretes various proteins into its extracellular milieu. Bioinformatics analyses have indicated that most of these proteins are directed to the canonical Sec pathway, which consists of the translocation motor SecA and a membrane-embedded channel composed of the SecY, SecE, and SecG proteins. In addition, S. aureus contains an accessory Sec2 pathway involving the SecA2 and SecY2 proteins. Here, we have addressed the roles of the nonessential channel components SecG and SecY2 in the biogenesis of the extracellular proteome of S. aureus. The results show that SecG is of major importance for protein secretion by S. aureus. Specifically, the extracellular accumulation of nine abundant exoproteins and seven cell wall-bound proteins was significantly affected in an secG mutant. No secretion defects were detected for strains with a secY2 single mutation. However, deletion of secY2 exacerbated the secretion defects of secG mutants, affecting the extracellular accumulation of one additional exoprotein and one cell wall protein. Furthermore, an secG secY2 double mutant displayed a synthetic growth defect. This might relate to a slightly elevated expression of sraP, encoding the only known substrate for the Sec2 pathway, in cells lacking SecG. Additionally, the results suggest that SecY2 can interact with the Sec1 channel, which would be consistent with the presence of a single set of secE and secG genes in S. aureus. doi: 10.1128/JB.01452-09

Published
2010

37. Diamide triggers mainly S thiolations in the cytoplasmic proteomes of Bacillus subtilis and Staphylococcus aureus

Author

Pother, Dierk-Christoph, Liebeke, Manuel, Hochgrafe, Falko, Antelmann, Haike, Becher, Dorte, Lalk, Michael, Lindequist, Ulrike, Borovok, Ilya, Cohen, Gerald, Aharonowitz, Yair, and Hecker, Michael

Subjects
Bacterial proteins -- Properties, Staphylococcus aureus -- Physiological aspects, Bacillus subtilis -- Physiological aspects, Biological sciences
Abstract

Glutathione constitutes a key player in the thiol redox buffer in many organisms. However, the gram-positive bacteria Bacillus subtilis and Staphylococcus aureus lack this low-molecular-weight thiol. Recently, we identified S-cysteinylated proteins in B. subtilis after treatment of cells with the disulfide-generating electrophile diamide. S-cysteinylation is thought to protect protein thiols against irreversible oxidation to sulfinic and sulfonic acids. Here we show that S thiolation occurs also in S. aureus proteins after exposure to diamide. We further analyzed the formation of inter- and intramolecular disulfide bonds in cytoplasmic proteins using diagonal nonreducing/ reducing sodium dodecyl sulfate gel electrophoresis. However, only a few proteins were identified that form inter- or intramolecular disulfide bonds under control and diamide stress conditions in B. subtilis and S. aureus. Depletion of the cysteine pool was concomitantly measured in B. subtilis using a metabolomics approach. Thus, the majority of reversible thiol modifications that were previously detected by two-dimensional gel fluorescence-based thiol modification assay are most likely based on S thiolations. Finally, we found that a glutathione-producing B. subtilis strain which expresses the Listeria monocytogenes gshF gene did not show enhanced oxidative stress resistance compared to the wild type. doi: 10.1128/JB.00937-09

Published
2009

38. The YvrI alternative [sigma] factor is essential for acid stress induction of oxalate decarboxylase in Bacillus subtilis

Author

MacLellan, Shawn R., Helmann, John D., and Antelmann, Haike

Subjects
Bacillus subtilis -- Physiological aspects, DNA binding proteins -- Properties, Biological sciences
Abstract

YvrI is a recently identified alternative [sigma] factor in Bacillus subtilis that requires the coactivator YvrHa to activate transcription. Previously, a strain engineered to overproduce YvrI was found to overproduce oxalate decarboxylase (OxdC), and further analysis identified three YvrI-activated promoters preceding the yvrI-yvrHa, yvrJ, and oxdC-yvrL operons. Independently, proteome analyses identified OxdC as a highly abundant, cell wall-associated protein that accumulated under acidic growth conditions. We show here that the accumulation of OxdC in the cell wall proteome under acidic growth conditions is absolutely dependent on YvrI and is correlated with enhanced transcription of both the yvrl-yvrHa and the oxdC-yvrL operons. Conversely, OxdC accumulates to a high level even under nonacidic growth conditions in cells lacking YvrL, a negative regulator of YvrI/YvrHa-dependent transcription. These results indicate that YvrI and its associated coregulators YvrHa and YvrL are required for the regulation of OxdC expression by acid stress. The high-level accumulation of OxdC depends, in part, on a strong oxdC promoter. A regulatory sequence with similarity to an upstream promoter element (UP) was identified upstream of the oxdC promoter and is required for high-level promoter activity. Conservation of the YvrI/YvrHa/YvrL regulatory system among related species allowed us to deduce an expanded consensus sequence for the compositionally unusual promoters recognized by this new [sigma] factor.

Published
2009

42. The density of negative charge in the cell wall influences two-component signal transduction in Bacillus subtilis

Author

Hyyrylainen, Hanne-Leena, Pietiainen, Milla, Lunden, Tuula, Ekman, Anna, Gardemeister, Marika, Murtomaki-Repo, Sanna, Antelmann, Haike, Hecker, Michael, Valmu, Leena, Sarvas, Matti, and Kontinen, Vesa P.

Subjects
Bacterial cell walls -- Research, Bacillus subtilis -- Genetic aspects, Bacillus subtilis -- Research, Alanine -- Research, Gene expression -- Research, Biological sciences
Abstract

The Dlt system modulates the density of negative charge in the cell wall of Gram-positive bacteria by substituting anionic polymers (wall and lipoteichoic acids) with D-alanine. The htrA and htrB genes, regulated by the CssRS two-component system (TCS) and encoding membrane-associated protein quality control proteases, were expressed at strongly decreased levels in a mutant with defective Dlt (dltD:: miniTn 10) as compared to the [dlt.sup.+] wild-type strain under a secretion stress condition (hypersecretion of AmyQ [alpha]-amylase). The level of HtrA protein in the extracellular proteome of the dltD mutant was decreased consistently. Expression from the promoter of the lialHGFSR (yvqlHGFEC) operon ([P.sub.lial]) is dependent on the LiaRS TCS. The Dlt defect increased the expression from [P.sub.lial] under two stress conditions, AmyQ hypersecretion and treatment with a cationic antimicrobial peptide (LL-37), but decreased the expression in vancomycin-treated cells. Furthermore, Dlt inactivation enhanced the expression of the YxdJK-regulated yxdL gene in LL-37-treated cells. The increased net negative charge of the cell wall seems to cause varied and opposite effects on the expression of CssRS-, LiaRS- and YxdJK-regulated genes under different stress conditions. The results suggest that TCSs which sense misfolded proteins or peptides are modulated by the density of negative charge in the cell wall. The density of negative charge on the outer surface of the cell membrane did not have a similar effect on TCSs.

Published
2007

43. The Industrial Organism Corynebacterium glutamicum Requires Mycothiol as Antioxidant to Resist Against Oxidative Stress in Bioreactor Cultivations

Author

Hartmann, Fabian Stefan Franz, Clermont, Lina, Ngoc Tung, Quach, Antelmann, Haike, Seibold, Gerd, Hartmann, Fabian Stefan Franz, Clermont, Lina, Ngoc Tung, Quach, Antelmann, Haike, and Seibold, Gerd

Abstract

In aerobic environments, bacteria are exposed to reactive oxygen species (ROS). To avoid an excess of ROS, microorganisms are equipped with powerful enzymatic and non-enzymatic antioxidants. Corynebacterium glutamicum, a widely used industrial platform organism, uses mycothiol (MSH) as major low molecular weight (LMW) thiol and non-enzymatic antioxidant. In aerobic bioreactor cultivations, C. glutamicum becomes exposed to oxygen concentrations surpassing the air saturation, which are supposed to constitute a challenge for the intracellular MSH redox balance. In this study, the role of MSH was investigated at different oxygen levels (pO2) in bioreactor cultivations in C. glutamicum. Despite the presence of other highly efficient antioxidant systems, such as catalase, the MSH deficient ΔmshC mutant was impaired in growth in bioreactor experiments performed at pO2 values of 30%. At a pO2 level of 20%, this growth defect was abolished, indicating a high susceptibility of the MSH-deficient mutant towards elevated oxygen concentrations. Bioreactor experiments with C. glutamicum expressing the Mrx1-roGFP2 redox biosensor revealed a strong oxidative shift in the MSH redox potential (EMSH) at pO2 values above 20%. This indicates that the LMW thiol MSH is an essential antioxidant to maintain the robustness and industrial performance of C. glutamicum during aerobic fermentation processes.

Published
2020

45. A disulfide bond-containing alkaline phosphatase triggers a BdbC-dependent secretion stress response in Bacillus subtilis

Author

Darmon, Elise, Dubois, Jean-Yves F, Van Dijl, Jan Maarten, Dorenbos, Ronald, Quax, Wim J., Meens, Jochen, Bron, Sierd, Freudl, Roland, Antelmann, Haike, and Hecker, Michael

Subjects
Bacillus subtilis -- Genetic aspects, Alkaline phosphatase -- Chemical properties, Secretion -- Research, Biological sciences
Abstract

An investigation on whether high-level production of a secretory protein with two disulfide bonds, PhoA of Escherichia coli, induces secretion stress in Bacillus subtilis is presented. Results reveal that Eschericia coli PhoA production triggers a relatively moderate CssRS-dependent secretion stress response in B. subtilis.

Published
2006

46. pSM19035-encoded [zeta] toxin induces stasis followed by death in a subpopulation of cells

Author

Lioy, Virginia S., Martin, M. Teresa, Camacho, Ana G., Lurz, Rudi, Antelmann, Haike, Hecker, Michael, Hitchin, Ed, Ridge, Yvonne, Wells, Jerry M., and Alonso, Juan C

Subjects
Escherichia coli -- Genetic aspects, Gene expression -- Research, Genetic code -- Research, Genetic research, Biological sciences
Abstract

The toxin-antitoxin operon of pSM19035 encodes three proteins: the [omega] global regulator, the [epsilon] labile antitoxin and the stable [zeta] toxin. Accumulation of [zeta] toxin free of [epsilon] antitoxin induced loss of cell proliferation in both Bacillus subtilis and Escherichia coli cells. Induction of a [zeta] variant ([zeta]Y83C) triggered stasis, in which B. subtilis cells were viable but unable to proliferate, without selectively affecting protein translation. In E. coli cells, accumulation of free [zeta] toxin induced stasis, but this was fully reversed by expression of the [epsilon] antitoxin within a defined time window. The time window for reversion of [zeta] toxicity by expression of [epsilon] antitoxin was dependent on the initial cellular level of [zeta]. After 240 min of constitutive expression, or inducible expression of high levels of [zeta] toxin for 30 min, expression of [epsilon] failed to reverse the toxic effect exerted by [zeta] in cells growing in minimal medium. Under the latter conditions, [zeta] inhibited replication, transcription and translation and finally induced death in a fraction (~ 50 %) of the cell population. These results support the view that [zeta] interacts with its specific target and reversibly inhibits cell proliferation, but accumulation of [zeta] might lead to cell death due to pleiotropic effects.

Published
2006

47. Role of the fur regulon in iron transport in Bacillus subtilis

Author

Ollinger, Juliane, Song, Kyung-Bok, Antelmann, Haike, Hecker, Michael, and Helmann, John D.

Subjects
Bacillus subtilis -- Genetic aspects, Repressor proteins -- Research, Adenosine triphosphatase -- Research, Biological sciences
Abstract

The Bacillus subtilis ferric uptake regulator (Fur) protein mediates the iron-dependent repression of at least 20 operons encoding ~40 genes. We investigated the physiological roles of Fur-regulated genes by the construction of null mutations in 14 transcription units known or predicted to function in siderophore biosynthesis or iron uptake. We demonstrate that ywbLMN, encoding an elemental iron uptake system orthologous to the copper oxidase-dependent Fe(III) uptake system of Saccharomyces cerevisiae, is essential for growth in Iow iron minimal medium lacking citric acid. 2,3-Dihydroxybenzoyl-glycine (Itoic acid), the siderophore precursor produced by laboratory strains of B. subtilis, is of secondary importance. In the presence of citrate, the YfmCDEF ABC transporter is required for optimal growth. B. subtilis is unable to grow in minimal medium containing the iron chelator EDDHA unless the ability to synthesize the intact bacillibactin siderophore is restored (by the introduction of a functional sfp gene) or exogenous siderophores are provided. Utilization of the catecholate siderophores bacillibactin and enterobactin requires the FeuABC importer and the YusV ATPase. Utilization of hydroxamate siderophores requires the FhuBGC ABC transporter together with the FhuD (ferrichrome) or YxeB (ferrioxamine) substrate-binding proteins. Growth with schizokinen or arthrobactin is at least partially dependent on the YfhA YfiYZ importer and the YusV ATPase. We have also investigated the effects of a fur mutation on the proteome and documented the derepression of 11 Fur-regulated proteins, including a newly identified thioredoxin reductase homolog, YcgT.

Published
2006

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