Zobrazeno 1 - 10
of 30
pro vyhledávání: '"MESH: Adhesins, Bacterial"'
Autor:
Lazar Ranin, Philippe Glaser, Claire Poyart, Ina Gajic, Céline Plainvert, Asmaa Tazi, Dusan Kekic, Nicolas Dmytruk, Vera Mijac, Natasa Opavski
Publikováno v:
International Journal of Medical Microbiology
International Journal of Medical Microbiology, Elsevier, 2019, 309 (1), pp.19-25. ⟨10.1016/j.ijmm.2018.10.005⟩
International Journal of Medical Microbiology, 2019, 309 (1), pp.19-25. ⟨10.1016/j.ijmm.2018.10.005⟩
International Journal of Medical Microbiology, Elsevier, 2019, 309 (1), pp.19-25. ⟨10.1016/j.ijmm.2018.10.005⟩
International Journal of Medical Microbiology, 2019, 309 (1), pp.19-25. ⟨10.1016/j.ijmm.2018.10.005⟩
International audience; Streptococcus agalactiae (group B Streptococcus, GBS) remains the leading cause of invasive diseases in neonates and an important cause of infections in the elderly. The aim of this study was to access the prevalence of GBS ge
Autor:
Cherry Gao, Patrick Trieu-Cuot, Claire Poyart, Bruno Périchon, Julie Guignot, Shaynoor Dramsi, Noémi Szili
Publikováno v:
Microbes and Infection
Microbes and Infection, Elsevier, 2019, 21 (2), pp.99-103. ⟨10.1016/j.micinf.2018.10.004⟩
Microbes and Infection, 2019, 21 (2), pp.99-103. ⟨10.1016/j.micinf.2018.10.004⟩
Microbes and Infection, Elsevier, 2019, 21 (2), pp.99-103. ⟨10.1016/j.micinf.2018.10.004⟩
Microbes and Infection, 2019, 21 (2), pp.99-103. ⟨10.1016/j.micinf.2018.10.004⟩
International audience; The core PI-2b pilus present in "hypervirulent" ST-17 Streptococcus agalactiae strains consists of three pilin subunits (Spb1, Ap1 and Ap2) assembled by sortase SrtC1 and cell-wall anchored by Srt2. Spb1 was shown to be the ma
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b7c425b2b9077d1b11a6b168b081969
https://hal-pasteur.archives-ouvertes.fr/pasteur-02863685/document
https://hal-pasteur.archives-ouvertes.fr/pasteur-02863685/document
Autor:
Olivera Francetic, Scott J. Hultgren, Henry L. Schreiber, Caitlin N. Spaulding, Karen W. Dodson, Weili Zheng, Pontus Svenmarker, Fengbin Wang, Edward H. Egelman, Jennie E Hazen, Magnus Andersson, Matt S. Conover, Areli Luna-Rico
Publikováno v:
eLife
eLife, eLife Sciences Publication, 2018, 7, pp.e31662. ⟨10.7554/eLife.31662⟩
eLife, Vol 7 (2018)
eLife, 2018, 7, pp.e31662. ⟨10.7554/eLife.31662⟩
eLife, eLife Sciences Publication, 2018, 7, pp.e31662. ⟨10.7554/eLife.31662⟩
eLife, Vol 7 (2018)
eLife, 2018, 7, pp.e31662. ⟨10.7554/eLife.31662⟩
Uropathogenic E. coli (UPEC), which cause urinary tract infections (UTI), utilize type 1 pili, a chaperone usher pathway (CUP) pilus, to cause UTI and colonize the gut. The pilus rod, comprised of repeating FimA subunits, provides a structural scaffo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6e8e13b6cd0e9b5e23ba08b4d46c2d1e
https://hal-pasteur.archives-ouvertes.fr/pasteur-02565620/document
https://hal-pasteur.archives-ouvertes.fr/pasteur-02565620/document
Autor:
Jenifer Coburn, Patrick England, Jacques Bellalou, Mathieu Picardeau, Hiromi Sato, Robert A. Gaultney, Azad Eshghi, Tara J. Moriarty, Sébastien Brûlé, Isabelle Miras, Ahmed Haouz
Publikováno v:
Cell Microbiol
Cellular Microbiology
Cellular Microbiology, Wiley, 2019, 21 (2), pp.e12949. ⟨10.1111/cmi.12949⟩
Cellular Microbiology, 2019, 21 (2), pp.e12949. ⟨10.1111/cmi.12949⟩
Cellular Microbiology
Cellular Microbiology, Wiley, 2019, 21 (2), pp.e12949. ⟨10.1111/cmi.12949⟩
Cellular Microbiology, 2019, 21 (2), pp.e12949. ⟨10.1111/cmi.12949⟩
International audience; Pathogenic Leptospira bacteria are the causative agents of leptospirosis, a zoonotic disease affecting animals and humans worldwide. These pathogenic species have the ability to rapidly cross host tissue barriers by a yet unkn
Autor:
Verena Königer, D. Scott Merrell, Roman Andriiovych Moskalenko, Rainer Haas, Thomas Borén, Sara Henriksson, Jafar Mahdavi, Abhijit Chowdhury, Johan Ögren, Anders Hofer, Jay V. Solnick, Dan Danielsson, Sara K. Lindén, Dag Ilver, Konstantinos S. Papadakos, Susanne Vikström, Jörgen Ådén, Jan Holgersson, Gerhard Gröbner, Alexej Schmidt, Jeanna Bugaytsova, Oscar Björnham, Göran O. Bylund, Rolf Sjöström, Stefan Oscarson, Dionyssios N. Sgouras, Lori M. Hansen, Yevgen A Chernov, Anders Esberg, Kristof Moonens, Christopher Aisenbrey, Charles Kelly, Ludmilla A. Morozova-Roche, Jeannette M. Whitmire, Beatriz Martinez-Gonzalez, Asish K. Mukhopadhyay, Angela Eldridge, Nicklas Strömberg, Robert H. Gilman, Andre Dubois, Lars Engstrand, Staffan Schedin, Brett A. Chromy, Justine Younson, Matthew Goldman, Anna Shevtsova, Macarena P. Quintana-Hayashi, Hui Liu, Magnus Unemo, Lena Rakhimova, Anna Åberg, Sebastian Suerbaum, Anna Arnqvist, Pär Gideonsson, Maréne Landström, Douglas E. Berg, Kristoffer Brännström, Anders Olofsson, Melissa Mendez, G. Balakrish Nair, Han Remaut
Publikováno v:
Cell Host and Microbe
Cell Host and Microbe, Elsevier, 2017, 21 (3), pp.376-389. ⟨10.1016/j.chom.2017.02.013⟩
Cell host & microbe, vol 21, iss 3
Bugaytsova, J A, Björnham, O, Chernov, Y A, Gideonsson, P, Henriksson, S, Mendez, M, Sjöström, R, Mahdavi, J, Shevtsova, A, Ilver, D, Moonens, K, Quintana-Hayashi, M P, Moskalenko, R, Aisenbrey, C, Bylund, G, Schmidt, A, Åberg, A, Brännström, K, Königer, V, Vikström, S, Rakhimova, L, Hofer, A, Ögren, J, Liu, H, Goldman, M D, Whitmire, J M, Ådén, J, Younson, J, Kelly, C G, Gilman, R H, Chowdhury, A, Mukhopadhyay, A K, Nair, G B, Papadakos, K S, Martinez-Gonzalez, B, Sgouras, D N, Engstrand, L, Unemo, M, Danielsson, D, Suerbaum, S, Oscarson, S, Morozova-Roche, L A, Olofsson, A, Gröbner, G, Holgersson, J, Esberg, A, Strömberg, N, Landström, M, Eldridge, A M, Chromy, B A, Hansen, L M, Solnick, J V, Lindén, S K, Haas, R, Dubois, A, Merrell, D S, Schedin, S, Remaut, H, Arnqvist, A, Berg, D E & Borén, T 2017, ' Helicobacter pylori Adapts to Chronic Infection and Gastric Disease via pH-Responsive BabA-Mediated Adherence ', Cell Host & Microbe, vol. 21, no. 3, pp. 376-389 . https://doi.org/10.1016/j.chom.2017.02.013
Cell Host and Microbe, Elsevier, 2017, 21 (3), pp.376-389. ⟨10.1016/j.chom.2017.02.013⟩
Cell host & microbe, vol 21, iss 3
Bugaytsova, J A, Björnham, O, Chernov, Y A, Gideonsson, P, Henriksson, S, Mendez, M, Sjöström, R, Mahdavi, J, Shevtsova, A, Ilver, D, Moonens, K, Quintana-Hayashi, M P, Moskalenko, R, Aisenbrey, C, Bylund, G, Schmidt, A, Åberg, A, Brännström, K, Königer, V, Vikström, S, Rakhimova, L, Hofer, A, Ögren, J, Liu, H, Goldman, M D, Whitmire, J M, Ådén, J, Younson, J, Kelly, C G, Gilman, R H, Chowdhury, A, Mukhopadhyay, A K, Nair, G B, Papadakos, K S, Martinez-Gonzalez, B, Sgouras, D N, Engstrand, L, Unemo, M, Danielsson, D, Suerbaum, S, Oscarson, S, Morozova-Roche, L A, Olofsson, A, Gröbner, G, Holgersson, J, Esberg, A, Strömberg, N, Landström, M, Eldridge, A M, Chromy, B A, Hansen, L M, Solnick, J V, Lindén, S K, Haas, R, Dubois, A, Merrell, D S, Schedin, S, Remaut, H, Arnqvist, A, Berg, D E & Borén, T 2017, ' Helicobacter pylori Adapts to Chronic Infection and Gastric Disease via pH-Responsive BabA-Mediated Adherence ', Cell Host & Microbe, vol. 21, no. 3, pp. 376-389 . https://doi.org/10.1016/j.chom.2017.02.013
The BabA adhesin mediates high-affinity binding of Helicobacter pylori to the ABO blood group antigen-glycosylated gastric mucosa. Here we show that BabA is acid responsive-binding is reduced at low pH and restored by acid neutralization. Acid respon
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a43b410aab75acc08a9fa79a43ec0bb
https://hal-riip.archives-ouvertes.fr/pasteur-02195957
https://hal-riip.archives-ouvertes.fr/pasteur-02195957
Autor:
Madhu Nagaraj, Marcella Orwick-Rydmark, Barth‐J. van Rossum, Michael Habeck, Benjamin Bardiaux, Shakeel A. Shahid, Trent W. Franks, Nandini Chauhan, Dirk Linke
Publikováno v:
Angewandte Chemie International Edition
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2015, 54 (43), pp.12602-12606. ⟨10.1002/anie.201505506⟩
Angewandte Chemie-International Edition
Angewandte Chemie International Edition, 2015, 54 (43), pp.12602-12606. ⟨10.1002/anie.201505506⟩
Angewandte Chemie International Edition, Wiley-VCH Verlag, 2015, 54 (43), pp.12602-12606. ⟨10.1002/anie.201505506⟩
Angewandte Chemie-International Edition
Angewandte Chemie International Edition, 2015, 54 (43), pp.12602-12606. ⟨10.1002/anie.201505506⟩
International audience; MAS-NMR was used to study the structure and dynamics at ambient temperatures of the membrane-anchor domain of YadA (YadA-M) in a pellet of the outer membrane of E. coli in which it was expressed. YadA is an adhesin from the pa
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::78dfa06f31892222f3e61b41275c6480
https://hal-pasteur.archives-ouvertes.fr/pasteur-01399310
https://hal-pasteur.archives-ouvertes.fr/pasteur-01399310
Autor:
Pietro Giorgio Lovaglio, Morgan Ledroit, Anna Carannante, Fabio Rigat, Maurizio Comanducci, Cecilia Fazio, Raquel Abad, Giacomo Frosi, Jamie Findlow, Dominique A. Caugant, Ulrich Vogel, Muhamed-Kheir Taha, John J. Donnelly, Duccio Medini, Jay Lucidarme, Danielle Thompson, Davide Serruto, Martin Musilek, Maria Stella, Stefanie Gilchrist, Alessandro Muzzi, Paola Stefanelli, Ala Eddine Deghmane, Luca Orlandi, Eva Hong, Stefania Bambini, Ray Borrow, Heike Claus, Giuseppe Boccadifuoco, Julio A. Vázquez, Marzia Monica Giuliani, Paula Kriz, Rino Rappuoli, Jan Oksnes, Matthias Frosch, Mariagrazia Pizza
Publikováno v:
The Lancet Infectious Diseases
The Lancet Infectious Diseases, New York, NY : Elsevier Science ; The Lancet Pub. Group, 2001-, 2013, 13 (5), pp.416-425. ⟨10.1016/S1473-3099(13)70006-9⟩
The Lancet Infectious Diseases, 2013, 13 (5), pp.416-425. ⟨10.1016/S1473-3099(13)70006-9⟩
The Lancet Infectious Diseases, New York, NY : Elsevier Science ; The Lancet Pub. Group, 2001-, 2013, 13 (5), pp.416-425. ⟨10.1016/S1473-3099(13)70006-9⟩
The Lancet Infectious Diseases, 2013, 13 (5), pp.416-425. ⟨10.1016/S1473-3099(13)70006-9⟩
Summary Background A novel multicomponent vaccine against meningococcal capsular group B (MenB) disease contains four major components: factor-H-binding protein, neisserial heparin binding antigen, neisserial adhesin A, and outer-membrane vesicles de
Autor:
Xiangan Han, Jacques Mainil, Renwei Wu, W. Florian Fricke, Shelley C. Rankin, François-Xavier Weill, Chunhong Zhu, Dieter M. Schifferli, Robert Schmieder, Shaohua Zhao, Robert Edwards, Nan Zhang, Leon De Masi, Patrick F. McDermott, Radhey S. Kaushik, Xun Ma, Min Yue, Cesar Arze, Junjie Zhang, George P. Fraser, Dustin Brisson
Publikováno v:
Nature Communications
Nature Communications, 2015, 6 (6), pp.8754. ⟨10.1038/ncomms9754⟩
Nature Communications, Nature Publishing Group, 2015, 6 (6), pp.8754. ⟨10.1038/ncomms9754⟩
Nature Communications, 2015, 6 (6), pp.8754. ⟨10.1038/ncomms9754⟩
Nature Communications, Nature Publishing Group, 2015, 6 (6), pp.8754. ⟨10.1038/ncomms9754⟩
Understanding the molecular parameters that regulate cross-species transmission and host adaptation of potential pathogens is crucial to control emerging infectious disease. Although microbial pathotype diversity is conventionally associated with gen
Autor:
Rosita De Paola, Eva Hong, Monica Moschioni, Izabela Waśko, Anna Skoczyńska, Muhamed-Kheir Taha, Maria Stella
Publikováno v:
Vaccine
Vaccine, 2016, 34 (4), pp.510-515. ⟨10.1016/j.vaccine.2015.11.070⟩
Vaccine, Elsevier, 2016, 34 (4), pp.510-515. ⟨10.1016/j.vaccine.2015.11.070⟩
Vaccine, 2016, 34 (4), pp.510-515. ⟨10.1016/j.vaccine.2015.11.070⟩
Vaccine, Elsevier, 2016, 34 (4), pp.510-515. ⟨10.1016/j.vaccine.2015.11.070⟩
International audience; Neisseria meningitidis of serogroup B (MenB) is currently responsible for more than 70% of cases of invasive meningococcal disease (IMD) in Poland and Europe as a whole. The aim of this study was to estimate strain coverage of
Autor:
Ernesto Cota, Alain L. Servin, Steve L. Moseley, Julie Guignot, Steve Matthews, Natalia Korotkova, Severine Monpouet, Yuri Lebedin
Publikováno v:
Journal of Biological Chemistry
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2006, 281 (39), pp.29120-30. ⟨10.1074/jbc.M605681200⟩
Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2006, 281 (39), pp.29120-30. ⟨10.1074/jbc.M605681200⟩
International audience; Escherichia coli expressing the Dr family of adhesins adheres to epithelial cells by binding to decay-accelerating factor (DAF) and carcinoembryonic antigen (CEA)-related cell surface proteins. The attachment of bacteria expre