Cargando…

GroEL is an immunodominant surface-exposed antigen of Rickettsia typhi

Rickettsioses are neglected and emerging potentially fatal febrile diseases that are caused by obligate intracellular bacteria, rickettsiae. Rickettsia (R.) typhi and R. prowazekii constitute the typhus group (TG) of rickettsiae and are the causative agents of endemic and epidemic typhus, respective...

Descripción completa

Detalles Bibliográficos
Autores principales:	Rauch, Jessica, Barton, Jessica, Kwiatkowski, Marcel, Wunderlich, Malte, Steffen, Pascal, Moderzynski, Kristin, Papp, Stefanie, Höhn, Katharina, Schwanke, Hella, Witt, Susanne, Richardt, Ulricke, Mehlhoop, Ute, Schlüter, Hartmut, Pianka, Verena, Fleischer, Bernhard, Tappe, Dennis, Osterloh, Anke
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Public Library of Science 2021
Materias:	Research Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8191997/ https://www.ncbi.nlm.nih.gov/pubmed/34111210 http://dx.doi.org/10.1371/journal.pone.0253084

Ejemplares similares

CD4(+) T Cells Are as Protective as CD8(+) T Cells against Rickettsia typhi Infection by Activating Macrophage Bactericidal Activity
por: Moderzynski, Kristin, et al.
Publicado: (2016)

Liver Necrosis and Lethal Systemic Inflammation in a Murine Model of Rickettsia typhi Infection: Role of Neutrophils, Macrophages and NK Cells
por: Papp, Stefanie, et al.
Publicado: (2016)

Cytotoxic effector functions of T cells are not required for protective immunity against fatal Rickettsia typhi infection in a murine model of infection: Role of T(H)1 and T(H)17 cytokines in protection and pathology
por: Moderzynski, Kristin, et al.
Publicado: (2017)

GFPuv-Expressing Recombinant Rickettsia typhi: a Useful Tool for the Study of Pathogenesis and CD8(+) T Cell Immunology in R. typhi Infection
por: Hauptmann, Matthias, et al.
Publicado: (2017)

Creating the Functional Single-Ring GroEL-GroES Chaperonin Systems via Modulating GroEL-GroES Interaction
por: Illingworth, Melissa, et al.
Publicado: (2017)

Myxococcus xanthus DK1622 Coordinates Expressions of the Duplicate groEL and Single groES Genes for Synergistic Functions of GroELs and GroES
por: Zhuo, Li, et al.
Publicado: (2017)

Back to GroEL-Assisted Protein Folding: GroES Binding-Induced Displacement of Denatured Proteins from GroEL to Bulk Solution
por: Marchenkov, Victor, et al.
Publicado: (2020)

Evaluation of PLGA-Encapsulated Recombinant GroEL of S. typhi immune Responses Against Enterohaemorrhagic and Enteropathogenic Escherichia coli
por: Parvane, Milad, et al.
Publicado: (2022)

Markov propagation of allosteric effects in biomolecular systems: application to GroEL–GroES
por: Chennubhotla, Chakra, et al.
Publicado: (2006)

Transient conformational remodeling of folding proteins by GroES—individually and in concert with GroEL
por: Moparthi, Satish Babu, et al.
Publicado: (2013)

Functional Differences between E. coli and ESKAPE Pathogen GroES/GroEL
por: Sivinski, Jared, et al.
Publicado: (2021)

Novel cryo-EM structure of an ADP-bound GroEL–GroES complex
por: Kudryavtseva, Sofia S., et al.
Publicado: (2021)

B-Cell Epitopes in GroEL of Francisella tularensis
por: Lu, Zhaohua, et al.
Publicado: (2014)

Dataset concerning GroEL chaperonin interaction with proteins
por: Marchenkov, V.V., et al.
Publicado: (2016)

Folding of maltose binding protein outside of and in GroEL
por: Ye, Xiang, et al.
Publicado: (2018)

Rickettsia typhi as Cause of Fatal Encephalitic Typhus in Hospitalized Patients, Hamburg, Germany, 1940–1944
por: Rauch, Jessica, et al.
Publicado: (2018)

Topologies of a Substrate Protein Bound to the Chaperonin GroEL
por: Elad, Nadav, et al.
Publicado: (2007)

Probing the Dynamic Process of Encapsulation in Escherichia coli GroEL
por: Mizuta, Toshifumi, et al.
Publicado: (2013)

Suppression of amyloid fibrils using the GroEL apical domain
por: Ojha, Bimlesh, et al.
Publicado: (2016)

Probing Water Density and Dynamics in the Chaperonin GroEL Cavity
por: Franck, John M., et al.
Publicado: (2014)

Structural and Computational Study of the GroEL–Prion Protein Complex
por: Mamchur, Aleksandra A., et al.
Publicado: (2021)

Folding of newly translated membrane protein CCR5 is assisted by the chaperonin GroEL-GroES
por: Chi, Haixia, et al.
Publicado: (2015)

In vivo client proteins of the chaperonin GroEL-GroES provide insight into the role of chaperones in protein evolution
por: Taguchi, Hideki, et al.
Publicado: (2023)

Self-assembly of the chaperonin GroEL nanocage induced at submicellar detergent
por: Chen, Jin, et al.
Publicado: (2014)

Immunization Using GroEL Decreases Clostridium difficile Intestinal Colonization
por: Péchiné, Séverine, et al.
Publicado: (2013)

Chaperonin GroEL Reassembly: An Effect of Protein Ligands and Solvent Composition
por: Ryabova, Nataliya, et al.
Publicado: (2014)

The Chaperonin GroEL: A Versatile Tool for Applied Biotechnology Platforms
por: O'Neil, Pierce T., et al.
Publicado: (2018)

Borrelia burgdorferi Surface Exposed GroEL Is a Multifunctional Protein
por: Cafiero, Thomas, et al.
Publicado: (2021)

GroEL Chaperonin-Based Assay for Early Diagnosis of Scrub Typhus
por: Indrawattana, Nitaya, et al.
Publicado: (2022)

Protein chain collapse modulation and folding stimulation by GroEL-ES
por: Naqvi, Mohsin M., et al.
Publicado: (2022)

Slowdown of Water Dynamics from the Top to the Bottom of the GroEL Cavity
por: Macro, Nicolas, et al.
Publicado: (2021)

GroEL—A Versatile Chaperone for Engineering and a Plethora of Applications
por: Yurkova, Maria S., et al.
Publicado: (2022)

GroEL-Proteotyping of Bacterial Communities Using Tandem Mass Spectrometry
por: Klaes, Simon, et al.
Publicado: (2023)

Multi-Scale Simulations Provide Supporting Evidence for the Hypothesis of Intramolecular Protein Translocation in GroEL/GroES Complexes
por: Coluzza, Ivan, et al.
Publicado: (2008)

The Mycobacterium tuberculosis sRNA F6 Modifies Expression of Essential Chaperonins, GroEL2 and GroES
por: Houghton, Joanna, et al.
Publicado: (2021)

GroEL as a molecular scaffold for structural analysis of the anthrax toxin pore
por: Katayama, Hiroo, et al.
Publicado: (2008)

Probing the Functional Mechanism of Escherichia coli GroEL Using Circular Permutation
por: Mizobata, Tomohiro, et al.
Publicado: (2011)

GroEL actively stimulates folding of the endogenous substrate protein PepQ
por: Weaver, Jeremy, et al.
Publicado: (2017)

Measuring protein stability in the GroEL chaperonin cage reveals massive destabilization
por: Korobko, Ilia, et al.
Publicado: (2020)

Production of a toxic polypeptide as a fusion inside GroEL cavity
por: Yurkova, Maria S., et al.
Publicado: (2020)

Cannot write session to /tmp/vufind_sessions/sess_8ropsn2g3g8un886mkeoruuebm