ArticleInfection and immunity1998
Subcellular localization and cytotoxic activity of the GroEL-like protein isolated from Actinobacillus actinomycetemcomitans.
Article in Infection and immunity, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
41 citing papers in PubMed, 129 citations in OpenAlex.
- Characterization of Molecular Chaperone GroEL as a Potential Virulence Factor inFoods (Basel, Switzerland) · 2023Article
- Outer Membrane Vesicles: Biogenesis, Functions, and Issues.Microbiology and molecular biology reviews : MMBR · 2022Review
- Review
- The Functional Differences between the GroEL Chaperonin ofBiomolecules · 2021Article
- Role of Hsp90 in Plasmodium falciparum Malaria.Advances in experimental medicine and biology · 2021Article
- A chemical inhibitor of heat shock protein 78 (HSP78) fromThe Journal of biological chemistry · 2020Article
- Proteomics of extracellular vesicles produced by Granulicatella adiacens, which causes infective endocarditis.PloS one · 2020Article
- Virulence and Pathogenicity Properties ofPathogens (Basel, Switzerland) · 2019Review
- Tools ofJournal of clinical medicine · 2019Review
- Proteomic Analysis and Virulence Assessment ofFrontiers in cellular and infection microbiology · 2019Article
- Comparative Genomic Analysis of Two Chilean Renibacterium salmoninarum Isolates and the Type Strain ATCC 33209T.Genome biology and evolution · 2018Article
- Synthesis and Self-Assembly of Chiral Cylindrical Molecular Complexes: Functional Heterogeneous Liquid-Solid Materials Formed by Helicene Oligomers.Molecules (Basel, Switzerland) · 2018Review
- Metabolic Adaptation of a C-Terminal Protease A-DeficientFrontiers in microbiology · 2017Article
- Plesiomonas shigelloides Revisited.Clinical microbiology reviews · 2016Review
- Intestinal M cells.Journal of biochemistry · 2016Review
- Bacterial Heat Shock Protein GroEL (Hsp64) Exerts Immunoregulatory Effects on T Cells by Utilizing Apoptosis.PloS one · 2016Article
- The GroEL protein of Porphyromonas gingivalis regulates atherogenic phenomena in endothelial cells mediated by upregulating toll-like receptor 4 expression.American journal of translational research · 2016Article
- IL12, IL10, IFNγ and TNFα Expression in Human Primary Monocytes Stimulated with Bacterial Heat Shock GroEL (Hsp64) Protein.PloS one · 2016Article
- Article
- Identification and Characterization of Anaplasma phagocytophilum Proteins Involved in Infection of the Tick Vector, Ixodes scapularis.PloS one · 2015Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The subcellular locations, ultrastructure, and cytotoxic activity of the GroEL-like protein from Actinobacillus actinomycetemcomitans were investigated. Two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) clearly indicated that synthesis of the GroEL-like protein is substantially increased after a thermal shock. Analysis of the purified native GroEL-like protein by transmission electron microscopy revealed the typical 14-mer cylindrical molecule, which had a diameter of about 12 nm. A. actinomycetemcomitans cells grown at 35 degreesC and heat shocked at 43 degreesC were fractionated, and fractions were separated by SDS-PAGE and analyzed by Western immunoblotting using antibodies to GroEL- and DnaK-like proteins. The GroEL-like protein was found in both the soluble and membrane fractions, whereas the DnaK-like protein was mostly found in the cytoplasm. An increase in specific proteins, including the GroEL- and DnaK-like proteins, was found in heat-shocked cells. The subcellular localization of the GroEL-like protein was examined by immunoelectron microscopy of whole cells. More GroEL-like protein was detected in stressed cells than in unstressed cells, and most of it was found not directly associated with outer membranes but rather in extracellular material. The native GroEL-like protein was assessed for cytotoxic activities. The GroEL-like protein increased the proliferation of periodontal ligament epithelial cells at concentrations between 0.4 and 1.0 microgram/ml. The number of cells in the culture decreased significantly at higher concentrations. A cell viability assay using HaCaT epithelial cells indicated that the GroEL-like protein was strongly toxic for the cells. These studies suggest the extracellular nature of the GroEL-like protein and its putative role in disease initiation.
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